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experiments in S. cerevisiae provided evidence that the pachytene checkpoint monitors and responds to recombinational DSB repair and synapsis independently. Wu and Burgess concluded that the repair checkpoint is RAD17-SAE2 dependent, while the synapsis checkpoint is PCH2-ZIP1 dependent [12]. Of these four genes, SAE2 and ZIP1 do not have clear mammalian orthologs (although SYCP1 may be a functional ortholog of ZIP1), and mutation of the mouse RAD17 ortholog, Rad1, presumably causes embryonic lethality [42]. Thus, mutational analysis of mouse Pch2 (Trip13), which is also critical for the synapsis checkpoint in C. elegans [2], was the best remaining option to evaluate potential functional conservation in mammalian meiotic checkpoint control.\nOur results demonstrate that in mice, the primary meiotic function of TRIP13 is in recombination itself. We found no evidence that it is involved in pachytene checkpoint control. Our data suggest that while recombination events destined to be resolved as COs can proceed normally in Trip13 mutants, DSBs that enter the NCO repair pathway are incompletely resolved or processed inefficiently. This hypothesis is compatible with current knowledge of meiotic recombination pathways. In S. cerevisiae, CO and NCO pathways are distinct [43]; they have different recombination intermediates, and are dependent upon different proteins [44,45]. Mice also appear to have independent CO versus NCO recombination pathways [46]. As in yeast, both require SPO11-induced breaks, but only the CO pathway requires MLH1. Both types of recombinant products are formed by mid-late pachynema. Another possibility is that the recombination defects are a result of defective intersister recombination. However, this type of DSB repair is suppressed in meiotic cells. Ablation of RAD54, which mediates intersister recombination in yeast, does not significantly disrupt meiosis in either yeast or mice [47,48]. Interestingly, RAD54-deficient spermatocytes display abnormal persistence of RAD51 foci on pachytene chromosomes, similar to those in TRIP13 mice, but there are no deleterious effects on meiotic progression or fertility [49].\nData from budding yeast also indicate that Pch2p functions in recombination. Deletion of PCH2 delays meiotic progression by ∼2 h in SK1 yeast, and causes a minor decrease in ascus formation [50]. DSBs persist \u003e2 h longer in pch2Δ yeast than in wild type, and hyperresection of DSBs in dmc1Δ pch2Δ double mutants is lower than in dmc1Δ cells [10]. Additionally, it was reported that pch2Δ yeast had a meiosis I delay dependent on the RAD17–SAE2 checkpoint that monitors recombination intermediates [12]. However, the exact role of TRIP13 (or Pch2) in recombination is unclear. Because synapsis occurs in TRIP13-deficient spermatocytes and is dependent on DSB formation (activity of SPO11 and MEI1), we suggest that TRIP13 functions after homology recognition and strand exchange, and that recombination events entering the CO repair pathway are either completed or nearly so (because OA treated resulted in bivalent chromosomes). One possibility for TRIP13′s role in recombination is that it is directly involved in a step specific to resolution of NCO recombination intermediates. Another possibility is that TRIP13 is required for disassembly of NCO recombinational repair complexes [51] containing those proteins that persist abnormally on Trip13Gt/Gt pachytene chromosomes. Notably, TRIP13 has two putative ATPase domains, a signature of AAA-ATPase ClpA/B chaperones that perform protein or protein/DNA complex disassembly [52]. These potential recombination roles might not be limited to meiosis, since Trip13 is widely transcribed and the mutant animals exhibited developmental defects. Finally, TRIP13 might play an indirect role, such as providing a “licensing” signal for the resolution of NCO intermediates and completion of meiosis.\nRegarding the cause of cell death in Trip13 mutants, our data indicate that this is triggered by defective DSB repair rather than asynapsis. We base this conclusion on two observations: (1) oocyte elimination is dependent upon DSB formation and (2) synapsis is normal in spermatocytes of adult testes. Indeed, this mutant is unique in that recombination defects occur in the absence of asynapsis (e.g., as in Dmc1 knockouts). Thus, the Trip13 mutant provides the first evidence that unrepaired DNA damage alone can trigger the mammalian pachytene checkpoint response. Furthermore, our results allow us to conclude that oocytes and spermatocytes share a similar, if not identical, DNA damage pachytene checkpoint that is decoupled from a synapsis checkpoint.\nInterestingly, we found that OA treatment of Trip13Gt/Gt spermatocytes could propel them into MI, despite a report that the same did not occur when wild-type pachytene spermatocytes were treated with the DSB-inducing agents gamma radiation or etoposide [53]. It is possible that the nascent induction of DSBs in pachynema evokes a checkpoint response that cannot be bypassed by OA, whereas the post-strand invasion lesions in TRIP13-deficient spermatocytes do not.\nTRIP13 was originally discovered to be an interactor with rat thyroid receptor beta (THRB; [54]), but the relationship between THRB and TRIP13 in meiosis is unknown. Interestingly, we observed that THRB is distributed diffusely throughout wild-type spermatocyte nuclei but is excluded from the XY (sex) body (unpublished observations), a compartmentalized nuclear domain beginning in pachynema, in which the sex chromosomes become heterochromatinized and transcriptionally silenced in the process of MSCI [55]. However, the XY body appeared intact in most mutant spermatocytes upon probing with several markers of XY heterochromatinization (unpublished observations). Considering that THRB knockout mice are viable and fertile [56], the functional relationship between TRIP13 and its receptor THRB in meiosis is unclear.\nGiven the high similarity of PCH2 orthologs throughout the eukaryotic world, one or more essential functions of this protein must be conserved. Since TRIP13 does not exhibit checkpoint function in mice, we surmise that the TRIP13/PCH2 ancestral protein had a function in recombination that persists to the present. Notably, A. thaliana does not appear to have a meiotic checkpoint activity that eliminates mutant meiocytes in a manner analogous to organisms such as mice, budding yeast, and female Drosophila [11,57], and mammalian TRIP13 is more similar to Arabidopsis PCH2 than the fly or worm proteins (Figures 1A and S1). The unusual relatedness between mammalian and plant PCH2 may therefore be attributable to both the presence of a common conserved function (namely recombination, although the role of PCH2 in plants has yet to be determined), and the absence of checkpoint function. Nevertheless, the evolutionary relationships between animals, fungi, and plants (which are discordant with PCH2 sequence phylogeny) do not allow parsimonious models addressing the points in time that checkpoint functions in PCH2 were gained or lost. It is possible that its checkpoint function evolved independently in worms and budding yeast. The picture will become clearer as the function of PCH2 in other organisms is elucidated.\nThe nature of the synapsis checkpoint in male mice remains unidentified. One possible candidate is Dot1 (PCH1 in yeast), a histone methyltransferase silencing factor that is required for pachytene arrest of zip1 and dmc1 mutants in yeast [58], and for preventing RAD54-mediated recombinational DSB repair between sister chromatids. However, DOT1 acts upstream of PCH2. Given that TRIP13 doesn't have checkpoint function in mice, a potential role for mammalian DOT1 in the pachytene checkpoint is dubious but awaits investigation. Recently, it was shown that the TRP53 homolog TRP63 is required for DNA damage–induced death of dictyate-stage primordial oocytes, leading to the suggestion that it is involved in monitoring genome integrity [59]. However, this activity occurs subsequent to a pachytene checkpoint. As alluded to earlier, a complicating problem for studying potential meiotic checkpoint genes in mice is that as in yeast, such genes often have mitotic functions (such as RAD24 [7]), and their ablation can cause lethality [42]. Unless mammalian pachytene checkpoint components have orthologs with similar functions in organisms such as yeast, their identities are likely to remain elusive."}

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experiments in S. cerevisiae provided evidence that the pachytene checkpoint monitors and responds to recombinational DSB repair and synapsis independently. Wu and Burgess concluded that the repair checkpoint is RAD17-SAE2 dependent, while the synapsis checkpoint is PCH2-ZIP1 dependent [12]. Of these four genes, SAE2 and ZIP1 do not have clear mammalian orthologs (although SYCP1 may be a functional ortholog of ZIP1), and mutation of the mouse RAD17 ortholog, Rad1, presumably causes embryonic lethality [42]. Thus, mutational analysis of mouse Pch2 (Trip13), which is also critical for the synapsis checkpoint in C. elegans [2], was the best remaining option to evaluate potential functional conservation in mammalian meiotic checkpoint control.\nOur results demonstrate that in mice, the primary meiotic function of TRIP13 is in recombination itself. We found no evidence that it is involved in pachytene checkpoint control. Our data suggest that while recombination events destined to be resolved as COs can proceed normally in Trip13 mutants, DSBs that enter the NCO repair pathway are incompletely resolved or processed inefficiently. This hypothesis is compatible with current knowledge of meiotic recombination pathways. In S. cerevisiae, CO and NCO pathways are distinct [43]; they have different recombination intermediates, and are dependent upon different proteins [44,45]. Mice also appear to have independent CO versus NCO recombination pathways [46]. As in yeast, both require SPO11-induced breaks, but only the CO pathway requires MLH1. Both types of recombinant products are formed by mid-late pachynema. Another possibility is that the recombination defects are a result of defective intersister recombination. However, this type of DSB repair is suppressed in meiotic cells. Ablation of RAD54, which mediates intersister recombination in yeast, does not significantly disrupt meiosis in either yeast or mice [47,48]. Interestingly, RAD54-deficient spermatocytes display abnormal persistence of RAD51 foci on pachytene chromosomes, similar to those in TRIP13 mice, but there are no deleterious effects on meiotic progression or fertility [49].\nData from budding yeast also indicate that Pch2p functions in recombination. Deletion of PCH2 delays meiotic progression by ∼2 h in SK1 yeast, and causes a minor decrease in ascus formation [50]. DSBs persist \u003e2 h longer in pch2Δ yeast than in wild type, and hyperresection of DSBs in dmc1Δ pch2Δ double mutants is lower than in dmc1Δ cells [10]. Additionally, it was reported that pch2Δ yeast had a meiosis I delay dependent on the RAD17–SAE2 checkpoint that monitors recombination intermediates [12]. However, the exact role of TRIP13 (or Pch2) in recombination is unclear. Because synapsis occurs in TRIP13-deficient spermatocytes and is dependent on DSB formation (activity of SPO11 and MEI1), we suggest that TRIP13 functions after homology recognition and strand exchange, and that recombination events entering the CO repair pathway are either completed or nearly so (because OA treated resulted in bivalent chromosomes). One possibility for TRIP13′s role in recombination is that it is directly involved in a step specific to resolution of NCO recombination intermediates. Another possibility is that TRIP13 is required for disassembly of NCO recombinational repair complexes [51] containing those proteins that persist abnormally on Trip13Gt/Gt pachytene chromosomes. Notably, TRIP13 has two putative ATPase domains, a signature of AAA-ATPase ClpA/B chaperones that perform protein or protein/DNA complex disassembly [52]. These potential recombination roles might not be limited to meiosis, since Trip13 is widely transcribed and the mutant animals exhibited developmental defects. Finally, TRIP13 might play an indirect role, such as providing a “licensing” signal for the resolution of NCO intermediates and completion of meiosis.\nRegarding the cause of cell death in Trip13 mutants, our data indicate that this is triggered by defective DSB repair rather than asynapsis. We base this conclusion on two observations: (1) oocyte elimination is dependent upon DSB formation and (2) synapsis is normal in spermatocytes of adult testes. Indeed, this mutant is unique in that recombination defects occur in the absence of asynapsis (e.g., as in Dmc1 knockouts). Thus, the Trip13 mutant provides the first evidence that unrepaired DNA damage alone can trigger the mammalian pachytene checkpoint response. Furthermore, our results allow us to conclude that oocytes and spermatocytes share a similar, if not identical, DNA damage pachytene checkpoint that is decoupled from a synapsis checkpoint.\nInterestingly, we found that OA treatment of Trip13Gt/Gt spermatocytes could propel them into MI, despite a report that the same did not occur when wild-type pachytene spermatocytes were treated with the DSB-inducing agents gamma radiation or etoposide [53]. It is possible that the nascent induction of DSBs in pachynema evokes a checkpoint response that cannot be bypassed by OA, whereas the post-strand invasion lesions in TRIP13-deficient spermatocytes do not.\nTRIP13 was originally discovered to be an interactor with rat thyroid receptor beta (THRB; [54]), but the relationship between THRB and TRIP13 in meiosis is unknown. Interestingly, we observed that THRB is distributed diffusely throughout wild-type spermatocyte nuclei but is excluded from the XY (sex) body (unpublished observations), a compartmentalized nuclear domain beginning in pachynema, in which the sex chromosomes become heterochromatinized and transcriptionally silenced in the process of MSCI [55]. However, the XY body appeared intact in most mutant spermatocytes upon probing with several markers of XY heterochromatinization (unpublished observations). Considering that THRB knockout mice are viable and fertile [56], the functional relationship between TRIP13 and its receptor THRB in meiosis is unclear.\nGiven the high similarity of PCH2 orthologs throughout the eukaryotic world, one or more essential functions of this protein must be conserved. Since TRIP13 does not exhibit checkpoint function in mice, we surmise that the TRIP13/PCH2 ancestral protein had a function in recombination that persists to the present. Notably, A. thaliana does not appear to have a meiotic checkpoint activity that eliminates mutant meiocytes in a manner analogous to organisms such as mice, budding yeast, and female Drosophila [11,57], and mammalian TRIP13 is more similar to Arabidopsis PCH2 than the fly or worm proteins (Figures 1A and S1). The unusual relatedness between mammalian and plant PCH2 may therefore be attributable to both the presence of a common conserved function (namely recombination, although the role of PCH2 in plants has yet to be determined), and the absence of checkpoint function. Nevertheless, the evolutionary relationships between animals, fungi, and plants (which are discordant with PCH2 sequence phylogeny) do not allow parsimonious models addressing the points in time that checkpoint functions in PCH2 were gained or lost. It is possible that its checkpoint function evolved independently in worms and budding yeast. The picture will become clearer as the function of PCH2 in other organisms is elucidated.\nThe nature of the synapsis checkpoint in male mice remains unidentified. One possible candidate is Dot1 (PCH1 in yeast), a histone methyltransferase silencing factor that is required for pachytene arrest of zip1 and dmc1 mutants in yeast [58], and for preventing RAD54-mediated recombinational DSB repair between sister chromatids. However, DOT1 acts upstream of PCH2. Given that TRIP13 doesn't have checkpoint function in mice, a potential role for mammalian DOT1 in the pachytene checkpoint is dubious but awaits investigation. Recently, it was shown that the TRP53 homolog TRP63 is required for DNA damage–induced death of dictyate-stage primordial oocytes, leading to the suggestion that it is involved in monitoring genome integrity [59]. However, this activity occurs subsequent to a pachytene checkpoint. As alluded to earlier, a complicating problem for studying potential meiotic checkpoint genes in mice is that as in yeast, such genes often have mitotic functions (such as RAD24 [7]), and their ablation can cause lethality [42]. Unless mammalian pachytene checkpoint components have orthologs with similar functions in organisms such as yeast, their identities are likely to remain elusive."}

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Wu and Burgess concluded that the repair checkpoint is RAD17-SAE2 dependent, while the synapsis checkpoint is PCH2-ZIP1 dependent [12]. Of these four genes, SAE2 and ZIP1 do not have clear mammalian orthologs (although SYCP1 may be a functional ortholog of ZIP1), and mutation of the mouse RAD17 ortholog, Rad1, presumably causes embryonic lethality [42]. Thus, mutational analysis of mouse Pch2 (Trip13), which is also critical for the synapsis checkpoint in C. elegans [2], was the best remaining option to evaluate potential functional conservation in mammalian meiotic checkpoint control.\nOur results demonstrate that in mice, the primary meiotic function of TRIP13 is in recombination itself. We found no evidence that it is involved in pachytene checkpoint control. Our data suggest that while recombination events destined to be resolved as COs can proceed normally in Trip13 mutants, DSBs that enter the NCO repair pathway are incompletely resolved or processed inefficiently. This hypothesis is compatible with current knowledge of meiotic recombination pathways. In S. cerevisiae, CO and NCO pathways are distinct [43]; they have different recombination intermediates, and are dependent upon different proteins [44,45]. Mice also appear to have independent CO versus NCO recombination pathways [46]. As in yeast, both require SPO11-induced breaks, but only the CO pathway requires MLH1. Both types of recombinant products are formed by mid-late pachynema. Another possibility is that the recombination defects are a result of defective intersister recombination. However, this type of DSB repair is suppressed in meiotic cells. Ablation of RAD54, which mediates intersister recombination in yeast, does not significantly disrupt meiosis in either yeast or mice [47,48]. Interestingly, RAD54-deficient spermatocytes display abnormal persistence of RAD51 foci on pachytene chromosomes, similar to those in TRIP13 mice, but there are no deleterious effects on meiotic progression or fertility [49].\nData from budding yeast also indicate that Pch2p functions in recombination. Deletion of PCH2 delays meiotic progression by ∼2 h in SK1 yeast, and causes a minor decrease in ascus formation [50]. DSBs persist \u003e2 h longer in pch2Δ yeast than in wild type, and hyperresection of DSBs in dmc1Δ pch2Δ double mutants is lower than in dmc1Δ cells [10]. Additionally, it was reported that pch2Δ yeast had a meiosis I delay dependent on the RAD17–SAE2 checkpoint that monitors recombination intermediates [12]. However, the exact role of TRIP13 (or Pch2) in recombination is unclear. Because synapsis occurs in TRIP13-deficient spermatocytes and is dependent on DSB formation (activity of SPO11 and MEI1), we suggest that TRIP13 functions after homology recognition and strand exchange, and that recombination events entering the CO repair pathway are either completed or nearly so (because OA treated resulted in bivalent chromosomes). One possibility for TRIP13′s role in recombination is that it is directly involved in a step specific to resolution of NCO recombination intermediates. Another possibility is that TRIP13 is required for disassembly of NCO recombinational repair complexes [51] containing those proteins that persist abnormally on Trip13Gt/Gt pachytene chromosomes. Notably, TRIP13 has two putative ATPase domains, a signature of AAA-ATPase ClpA/B chaperones that perform protein or protein/DNA complex disassembly [52]. These potential recombination roles might not be limited to meiosis, since Trip13 is widely transcribed and the mutant animals exhibited developmental defects. Finally, TRIP13 might play an indirect role, such as providing a “licensing” signal for the resolution of NCO intermediates and completion of meiosis.\nRegarding the cause of cell death in Trip13 mutants, our data indicate that this is triggered by defective DSB repair rather than asynapsis. We base this conclusion on two observations: (1) oocyte elimination is dependent upon DSB formation and (2) synapsis is normal in spermatocytes of adult testes. Indeed, this mutant is unique in that recombination defects occur in the absence of asynapsis (e.g., as in Dmc1 knockouts). Thus, the Trip13 mutant provides the first evidence that unrepaired DNA damage alone can trigger the mammalian pachytene checkpoint response. Furthermore, our results allow us to conclude that oocytes and spermatocytes share a similar, if not identical, DNA damage pachytene checkpoint that is decoupled from a synapsis checkpoint.\nInterestingly, we found that OA treatment of Trip13Gt/Gt spermatocytes could propel them into MI, despite a report that the same did not occur when wild-type pachytene spermatocytes were treated with the DSB-inducing agents gamma radiation or etoposide [53]. It is possible that the nascent induction of DSBs in pachynema evokes a checkpoint response that cannot be bypassed by OA, whereas the post-strand invasion lesions in TRIP13-deficient spermatocytes do not.\nTRIP13 was originally discovered to be an interactor with rat thyroid receptor beta (THRB; [54]), but the relationship between THRB and TRIP13 in meiosis is unknown. Interestingly, we observed that THRB is distributed diffusely throughout wild-type spermatocyte nuclei but is excluded from the XY (sex) body (unpublished observations), a compartmentalized nuclear domain beginning in pachynema, in which the sex chromosomes become heterochromatinized and transcriptionally silenced in the process of MSCI [55]. However, the XY body appeared intact in most mutant spermatocytes upon probing with several markers of XY heterochromatinization (unpublished observations). Considering that THRB knockout mice are viable and fertile [56], the functional relationship between TRIP13 and its receptor THRB in meiosis is unclear.\nGiven the high similarity of PCH2 orthologs throughout the eukaryotic world, one or more essential functions of this protein must be conserved. Since TRIP13 does not exhibit checkpoint function in mice, we surmise that the TRIP13/PCH2 ancestral protein had a function in recombination that persists to the present. Notably, A. thaliana does not appear to have a meiotic checkpoint activity that eliminates mutant meiocytes in a manner analogous to organisms such as mice, budding yeast, and female Drosophila [11,57], and mammalian TRIP13 is more similar to Arabidopsis PCH2 than the fly or worm proteins (Figures 1A and S1). The unusual relatedness between mammalian and plant PCH2 may therefore be attributable to both the presence of a common conserved function (namely recombination, although the role of PCH2 in plants has yet to be determined), and the absence of checkpoint function. Nevertheless, the evolutionary relationships between animals, fungi, and plants (which are discordant with PCH2 sequence phylogeny) do not allow parsimonious models addressing the points in time that checkpoint functions in PCH2 were gained or lost. It is possible that its checkpoint function evolved independently in worms and budding yeast. The picture will become clearer as the function of PCH2 in other organisms is elucidated.\nThe nature of the synapsis checkpoint in male mice remains unidentified. One possible candidate is Dot1 (PCH1 in yeast), a histone methyltransferase silencing factor that is required for pachytene arrest of zip1 and dmc1 mutants in yeast [58], and for preventing RAD54-mediated recombinational DSB repair between sister chromatids. However, DOT1 acts upstream of PCH2. Given that TRIP13 doesn't have checkpoint function in mice, a potential role for mammalian DOT1 in the pachytene checkpoint is dubious but awaits investigation. Recently, it was shown that the TRP53 homolog TRP63 is required for DNA damage–induced death of dictyate-stage primordial oocytes, leading to the suggestion that it is involved in monitoring genome integrity [59]. However, this activity occurs subsequent to a pachytene checkpoint. As alluded to earlier, a complicating problem for studying potential meiotic checkpoint genes in mice is that as in yeast, such genes often have mitotic functions (such as RAD24 [7]), and their ablation can cause lethality [42]. Unless mammalian pachytene checkpoint components have orthologs with similar functions in organisms such as yeast, their identities are likely to remain elusive."}

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experiments in S. cerevisiae provided evidence that the pachytene checkpoint monitors and responds to recombinational DSB repair and synapsis independently. Wu and Burgess concluded that the repair checkpoint is RAD17-SAE2 dependent, while the synapsis checkpoint is PCH2-ZIP1 dependent [12]. Of these four genes, SAE2 and ZIP1 do not have clear mammalian orthologs (although SYCP1 may be a functional ortholog of ZIP1), and mutation of the mouse RAD17 ortholog, Rad1, presumably causes embryonic lethality [42]. Thus, mutational analysis of mouse Pch2 (Trip13), which is also critical for the synapsis checkpoint in C. elegans [2], was the best remaining option to evaluate potential functional conservation in mammalian meiotic checkpoint control.\nOur results demonstrate that in mice, the primary meiotic function of TRIP13 is in recombination itself. We found no evidence that it is involved in pachytene checkpoint control. Our data suggest that while recombination events destined to be resolved as COs can proceed normally in Trip13 mutants, DSBs that enter the NCO repair pathway are incompletely resolved or processed inefficiently. This hypothesis is compatible with current knowledge of meiotic recombination pathways. In S. cerevisiae, CO and NCO pathways are distinct [43]; they have different recombination intermediates, and are dependent upon different proteins [44,45]. Mice also appear to have independent CO versus NCO recombination pathways [46]. As in yeast, both require SPO11-induced breaks, but only the CO pathway requires MLH1. Both types of recombinant products are formed by mid-late pachynema. Another possibility is that the recombination defects are a result of defective intersister recombination. However, this type of DSB repair is suppressed in meiotic cells. Ablation of RAD54, which mediates intersister recombination in yeast, does not significantly disrupt meiosis in either yeast or mice [47,48]. Interestingly, RAD54-deficient spermatocytes display abnormal persistence of RAD51 foci on pachytene chromosomes, similar to those in TRIP13 mice, but there are no deleterious effects on meiotic progression or fertility [49].\nData from budding yeast also indicate that Pch2p functions in recombination. Deletion of PCH2 delays meiotic progression by ∼2 h in SK1 yeast, and causes a minor decrease in ascus formation [50]. DSBs persist \u003e2 h longer in pch2Δ yeast than in wild type, and hyperresection of DSBs in dmc1Δ pch2Δ double mutants is lower than in dmc1Δ cells [10]. Additionally, it was reported that pch2Δ yeast had a meiosis I delay dependent on the RAD17–SAE2 checkpoint that monitors recombination intermediates [12]. However, the exact role of TRIP13 (or Pch2) in recombination is unclear. Because synapsis occurs in TRIP13-deficient spermatocytes and is dependent on DSB formation (activity of SPO11 and MEI1), we suggest that TRIP13 functions after homology recognition and strand exchange, and that recombination events entering the CO repair pathway are either completed or nearly so (because OA treated resulted in bivalent chromosomes). One possibility for TRIP13′s role in recombination is that it is directly involved in a step specific to resolution of NCO recombination intermediates. Another possibility is that TRIP13 is required for disassembly of NCO recombinational repair complexes [51] containing those proteins that persist abnormally on Trip13Gt/Gt pachytene chromosomes. Notably, TRIP13 has two putative ATPase domains, a signature of AAA-ATPase ClpA/B chaperones that perform protein or protein/DNA complex disassembly [52]. These potential recombination roles might not be limited to meiosis, since Trip13 is widely transcribed and the mutant animals exhibited developmental defects. Finally, TRIP13 might play an indirect role, such as providing a “licensing” signal for the resolution of NCO intermediates and completion of meiosis.\nRegarding the cause of cell death in Trip13 mutants, our data indicate that this is triggered by defective DSB repair rather than asynapsis. We base this conclusion on two observations: (1) oocyte elimination is dependent upon DSB formation and (2) synapsis is normal in spermatocytes of adult testes. Indeed, this mutant is unique in that recombination defects occur in the absence of asynapsis (e.g., as in Dmc1 knockouts). Thus, the Trip13 mutant provides the first evidence that unrepaired DNA damage alone can trigger the mammalian pachytene checkpoint response. Furthermore, our results allow us to conclude that oocytes and spermatocytes share a similar, if not identical, DNA damage pachytene checkpoint that is decoupled from a synapsis checkpoint.\nInterestingly, we found that OA treatment of Trip13Gt/Gt spermatocytes could propel them into MI, despite a report that the same did not occur when wild-type pachytene spermatocytes were treated with the DSB-inducing agents gamma radiation or etoposide [53]. It is possible that the nascent induction of DSBs in pachynema evokes a checkpoint response that cannot be bypassed by OA, whereas the post-strand invasion lesions in TRIP13-deficient spermatocytes do not.\nTRIP13 was originally discovered to be an interactor with rat thyroid receptor beta (THRB; [54]), but the relationship between THRB and TRIP13 in meiosis is unknown. Interestingly, we observed that THRB is distributed diffusely throughout wild-type spermatocyte nuclei but is excluded from the XY (sex) body (unpublished observations), a compartmentalized nuclear domain beginning in pachynema, in which the sex chromosomes become heterochromatinized and transcriptionally silenced in the process of MSCI [55]. However, the XY body appeared intact in most mutant spermatocytes upon probing with several markers of XY heterochromatinization (unpublished observations). Considering that THRB knockout mice are viable and fertile [56], the functional relationship between TRIP13 and its receptor THRB in meiosis is unclear.\nGiven the high similarity of PCH2 orthologs throughout the eukaryotic world, one or more essential functions of this protein must be conserved. Since TRIP13 does not exhibit checkpoint function in mice, we surmise that the TRIP13/PCH2 ancestral protein had a function in recombination that persists to the present. Notably, A. thaliana does not appear to have a meiotic checkpoint activity that eliminates mutant meiocytes in a manner analogous to organisms such as mice, budding yeast, and female Drosophila [11,57], and mammalian TRIP13 is more similar to Arabidopsis PCH2 than the fly or worm proteins (Figures 1A and S1). The unusual relatedness between mammalian and plant PCH2 may therefore be attributable to both the presence of a common conserved function (namely recombination, although the role of PCH2 in plants has yet to be determined), and the absence of checkpoint function. Nevertheless, the evolutionary relationships between animals, fungi, and plants (which are discordant with PCH2 sequence phylogeny) do not allow parsimonious models addressing the points in time that checkpoint functions in PCH2 were gained or lost. It is possible that its checkpoint function evolved independently in worms and budding yeast. The picture will become clearer as the function of PCH2 in other organisms is elucidated.\nThe nature of the synapsis checkpoint in male mice remains unidentified. One possible candidate is Dot1 (PCH1 in yeast), a histone methyltransferase silencing factor that is required for pachytene arrest of zip1 and dmc1 mutants in yeast [58], and for preventing RAD54-mediated recombinational DSB repair between sister chromatids. However, DOT1 acts upstream of PCH2. Given that TRIP13 doesn't have checkpoint function in mice, a potential role for mammalian DOT1 in the pachytene checkpoint is dubious but awaits investigation. Recently, it was shown that the TRP53 homolog TRP63 is required for DNA damage–induced death of dictyate-stage primordial oocytes, leading to the suggestion that it is involved in monitoring genome integrity [59]. However, this activity occurs subsequent to a pachytene checkpoint. As alluded to earlier, a complicating problem for studying potential meiotic checkpoint genes in mice is that as in yeast, such genes often have mitotic functions (such as RAD24 [7]), and their ablation can cause lethality [42]. Unless mammalian pachytene checkpoint components have orthologs with similar functions in organisms such as yeast, their identities are likely to remain elusive."}