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the present study, we identified a novel gene, mr-s, which is predominantly expressed in retinal photoreceptors and the pineal gland. The peak of mr-s expression in the developing retina is around P6. This expression pattern correlates with the rapid increase of Crx, rhodopsin and other photoreceptor genes around P6-P8. Around P6, the outer plexiform layer becomes visible and the outer layer of retina separates into two layers, ONL and INL. At the same time, photoreceptors begin to undergo terminal differentiation, forming the outer segment. We therefore hypothesized that mr-s is a key molecule in the late development of photoreceptors.\nWe previously reported that Otx2 and Crx have a critical role in photoreceptor development and that Otx2 directly regulates Crx transcription [3,9]. In situ hybridization and RT-PCR showed significant reduction of mr-s signal in the Crx KO retina and pineal gland. Furthermore, the luciferase assay demonstrated that Otx2 and Crx may directly upregulate the transcription of mr-s in mammalian cells. In retinal photoreceptor cells, the Otx2 transcripts are not highly expressed at P6-P9, while the Crx transcripts are strongly detected around P6. Therefore, our results strongly suggest that mr-s transcription is directly regulated by Crx. In the present study, Nrl, a photoreceptor-specific transcription factor that is highly expressed in photoreceptors at the postnatal stage, did not affect the transcription of mr-s. This finding is actually consistent with the analysis of the Nrl KO mouse which was recently reported [40]. The expression profiles of wild-type and Nrl KO retinas at P2, P10 and 2 months were analyzed and mr-s was not included in 161 differentially expressed genes in the Nrl KO retina.\nPrevious reports suggested that the SAM domain is a protein-protein interaction module. The SAM domain of the mr-s protein is closely related to that of ph and TEL, whose SAM domains can form a helical, head-to-tail polymeric structure and mediate the formation of a higher order chromatin structure. To characterize the biochemical function of mr-s, we performed yeast two-hybrid screening using full-length mr-s as the bait. As a result, the most frequent positive clones (5/28) in the screening were the cDNA fragments containing the SAM domain of mr-s. This strongly suggests that mr-s self-associates through its SAM domain. An immunoprecipitation assay, using two site-directed mutants of the SAM domain of mr-s, demonstrated that the mr-s protein can self-associate through its SAM domain in mammalian cells. While we did not address the question whether the SAM domain of mr-s forms a polymeric structure in the present study, the phylogenetic analysis of SAM domain of mr-s and other SAM domain-containing molecules suggests that mr-s can form head-to-tail polymer and mediate gene silencing by spreading repressive complexes along the chromatin similar to ph and/or TEL. Although our results in the immunoprecipitation assay demonstrated that the N-terminal constructs lacking a SAM domain still interact with each other, these results do not fit into the head-to-tail polymer model. We cannot exclude the possibility that the resulting protein-protein interaction of mr-s is an artifact of the overexpression conditions. The issue of whether or not mr-s forms a polymer awaits future analysis.\nA previous report indicated that TEL contains a sequence-specific DNA binding domain, namely the ETS domain, and binds to specific sites via its ETS domain [41]. TEL could serve to nucleate a polymer, which would spread by oligomerization of the SAM domain. In contrast to TEL, ph does not contain an obvious sequence-specific DNA binding motif (16). Therefore, its initial binding to the template may require protein-protein interactions with other sequence-specific transcriptional repressors. The segmentation gene-encoding transcriptional repressors such as Hunchback have a role in recruiting SAM domain-containing PcG proteins, which can spread along the template via polymerization [42]. Since mr-s does not contain obvious DNA binding motifs, we suppose that there is a sequence-specific transcription factor(s) which interacts with mr-s. However, we did not find any transcription factors in the present yeast two-hybrid screening.\nWe also found that full-length mr-s fused to the GAL4 DNA binding domain (DBD-mrs) functions as a transcriptional repressor. This may support the idea that mr-s is involved in repressive complexes similar to other SAM domain-containing proteins. Our results, however, showed that the self-association of mr-s through its SAM domain is not essential for the transcriptional repressive activity. Polymerization of the SAM domain has been previously reported to be essential for the repressive functions of ph and TEL [43,44]. On the other hand, human lethal(3) malignant brain tumor (H-L(3)MBT) protein, which also contains a SAM domain at the C-terminus, was reported as a transcriptional repressor and the repressor activity of H-L(3)MBT required mainly the presence of the MBT repeats but not the SAM domain [45]. To determine the transcriptional repressor region of the mr-s protein, we performed a luciferase assay using site-directed mutants (DBD-W404A and DBD-G453A). The result showed that the reduced binding ability of self-association partially compromises the transcriptional repressive activity of mr-s (Fig. 7D). However, the repressive effect was more significant when DBD-tail, which does not contain SAM domain, was co-introduced with the 5xGAL4-pGL3 reporter plasmid. Therefore, we conclude that a region from amino acids 463 to 542 is mainly responsible for the repressor activity in the case of mr-s. Evolutionary conservation of the C-terminal 80 aa region of mr-s from zebrafish through human may underlie the functional importance of this region.\nTwo distinct multiprotein PcG complexes, PRC1 and PRC2, have been identified. PRC2 is involved in the initiation of silencing and contains histone deacetylases (HDACs) and histone methyltransferases, which can methylate histone H3 lysine 9 and 27, marks of silenced chromatin. PRC1, including ph, recognizes the histone H3 lysine 27 mark set by PRC2 and maintains a stable state of gene repression in which PRC1 blocks chromatin remodeling by the trithorax group-related SWI-SNF complex [46,47]. Therefore, the mechanism of repression by PRC2 is thought to be HDAC-dependent while the mechanism of repression by PRC1 appears to be HDAC-independent. Our luciferase assay also showed that transcriptional repression of DBD-mrs was not affected by the addition of various concentrations of trichostatin A, a potent HDAC inhibitor (data not shown). Therefore, we speculate that the mechanism of repression of mr-s may be HDAC-independent and more similar to that of PRC1 complex.\nIn the present study, the biochemical experiments demonstrate that the mr-s protein functions as a transcriptional repressor and possibly down-regulates the spatial and temporal expression of the target genes during retinal photoreceptor development. Our data also revealed that the repressive activity of mr-s is mainly due to the C-terminal region (amino acids 463 to 542). However, downstream targets of mr-s still remain unclear. In situ hybridization showed that the peak of mr-s expression is around P6, when retinal photoreceptors undergo terminal differentiation. We hypothesize that the target genes of mr-s might be non-photoreceptor genes. In this case, mr-s may suppress the expression of non-photoreceptor genes in rod and cone photoreceptors. There may be another possibility that mr-s is involved in cell fate determination of rod photoreceptors versus cone photoreceptors. While cone photoreceptors are born during the early embryonic stages of mouse retinogenesis, rod photoreceptors are born primarily in the late embryonic and early postnatal period [48]. The expression pattern of mr-s may suggest that mr-s is expressed in rod photoreceptors but not in cone photoreceptors as well as Nr2e3, which is known as a transcriptional repressor and is thought to down-regulate cone photoreceptor-specific genes. To clarify the biological function of mr-s, analysis of mice with targeted disruptions of mr-s will be very important."}

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the present study, we identified a novel gene, mr-s, which is predominantly expressed in retinal photoreceptors and the pineal gland. The peak of mr-s expression in the developing retina is around P6. This expression pattern correlates with the rapid increase of Crx, rhodopsin and other photoreceptor genes around P6-P8. Around P6, the outer plexiform layer becomes visible and the outer layer of retina separates into two layers, ONL and INL. At the same time, photoreceptors begin to undergo terminal differentiation, forming the outer segment. We therefore hypothesized that mr-s is a key molecule in the late development of photoreceptors.\nWe previously reported that Otx2 and Crx have a critical role in photoreceptor development and that Otx2 directly regulates Crx transcription [3,9]. In situ hybridization and RT-PCR showed significant reduction of mr-s signal in the Crx KO retina and pineal gland. Furthermore, the luciferase assay demonstrated that Otx2 and Crx may directly upregulate the transcription of mr-s in mammalian cells. In retinal photoreceptor cells, the Otx2 transcripts are not highly expressed at P6-P9, while the Crx transcripts are strongly detected around P6. Therefore, our results strongly suggest that mr-s transcription is directly regulated by Crx. In the present study, Nrl, a photoreceptor-specific transcription factor that is highly expressed in photoreceptors at the postnatal stage, did not affect the transcription of mr-s. This finding is actually consistent with the analysis of the Nrl KO mouse which was recently reported [40]. The expression profiles of wild-type and Nrl KO retinas at P2, P10 and 2 months were analyzed and mr-s was not included in 161 differentially expressed genes in the Nrl KO retina.\nPrevious reports suggested that the SAM domain is a protein-protein interaction module. The SAM domain of the mr-s protein is closely related to that of ph and TEL, whose SAM domains can form a helical, head-to-tail polymeric structure and mediate the formation of a higher order chromatin structure. To characterize the biochemical function of mr-s, we performed yeast two-hybrid screening using full-length mr-s as the bait. As a result, the most frequent positive clones (5/28) in the screening were the cDNA fragments containing the SAM domain of mr-s. This strongly suggests that mr-s self-associates through its SAM domain. An immunoprecipitation assay, using two site-directed mutants of the SAM domain of mr-s, demonstrated that the mr-s protein can self-associate through its SAM domain in mammalian cells. While we did not address the question whether the SAM domain of mr-s forms a polymeric structure in the present study, the phylogenetic analysis of SAM domain of mr-s and other SAM domain-containing molecules suggests that mr-s can form head-to-tail polymer and mediate gene silencing by spreading repressive complexes along the chromatin similar to ph and/or TEL. Although our results in the immunoprecipitation assay demonstrated that the N-terminal constructs lacking a SAM domain still interact with each other, these results do not fit into the head-to-tail polymer model. We cannot exclude the possibility that the resulting protein-protein interaction of mr-s is an artifact of the overexpression conditions. The issue of whether or not mr-s forms a polymer awaits future analysis.\nA previous report indicated that TEL contains a sequence-specific DNA binding domain, namely the ETS domain, and binds to specific sites via its ETS domain [41]. TEL could serve to nucleate a polymer, which would spread by oligomerization of the SAM domain. In contrast to TEL, ph does not contain an obvious sequence-specific DNA binding motif (16). Therefore, its initial binding to the template may require protein-protein interactions with other sequence-specific transcriptional repressors. The segmentation gene-encoding transcriptional repressors such as Hunchback have a role in recruiting SAM domain-containing PcG proteins, which can spread along the template via polymerization [42]. Since mr-s does not contain obvious DNA binding motifs, we suppose that there is a sequence-specific transcription factor(s) which interacts with mr-s. However, we did not find any transcription factors in the present yeast two-hybrid screening.\nWe also found that full-length mr-s fused to the GAL4 DNA binding domain (DBD-mrs) functions as a transcriptional repressor. This may support the idea that mr-s is involved in repressive complexes similar to other SAM domain-containing proteins. Our results, however, showed that the self-association of mr-s through its SAM domain is not essential for the transcriptional repressive activity. Polymerization of the SAM domain has been previously reported to be essential for the repressive functions of ph and TEL [43,44]. On the other hand, human lethal(3) malignant brain tumor (H-L(3)MBT) protein, which also contains a SAM domain at the C-terminus, was reported as a transcriptional repressor and the repressor activity of H-L(3)MBT required mainly the presence of the MBT repeats but not the SAM domain [45]. To determine the transcriptional repressor region of the mr-s protein, we performed a luciferase assay using site-directed mutants (DBD-W404A and DBD-G453A). The result showed that the reduced binding ability of self-association partially compromises the transcriptional repressive activity of mr-s (Fig. 7D). However, the repressive effect was more significant when DBD-tail, which does not contain SAM domain, was co-introduced with the 5xGAL4-pGL3 reporter plasmid. Therefore, we conclude that a region from amino acids 463 to 542 is mainly responsible for the repressor activity in the case of mr-s. Evolutionary conservation of the C-terminal 80 aa region of mr-s from zebrafish through human may underlie the functional importance of this region.\nTwo distinct multiprotein PcG complexes, PRC1 and PRC2, have been identified. PRC2 is involved in the initiation of silencing and contains histone deacetylases (HDACs) and histone methyltransferases, which can methylate histone H3 lysine 9 and 27, marks of silenced chromatin. PRC1, including ph, recognizes the histone H3 lysine 27 mark set by PRC2 and maintains a stable state of gene repression in which PRC1 blocks chromatin remodeling by the trithorax group-related SWI-SNF complex [46,47]. Therefore, the mechanism of repression by PRC2 is thought to be HDAC-dependent while the mechanism of repression by PRC1 appears to be HDAC-independent. Our luciferase assay also showed that transcriptional repression of DBD-mrs was not affected by the addition of various concentrations of trichostatin A, a potent HDAC inhibitor (data not shown). Therefore, we speculate that the mechanism of repression of mr-s may be HDAC-independent and more similar to that of PRC1 complex.\nIn the present study, the biochemical experiments demonstrate that the mr-s protein functions as a transcriptional repressor and possibly down-regulates the spatial and temporal expression of the target genes during retinal photoreceptor development. Our data also revealed that the repressive activity of mr-s is mainly due to the C-terminal region (amino acids 463 to 542). However, downstream targets of mr-s still remain unclear. In situ hybridization showed that the peak of mr-s expression is around P6, when retinal photoreceptors undergo terminal differentiation. We hypothesize that the target genes of mr-s might be non-photoreceptor genes. In this case, mr-s may suppress the expression of non-photoreceptor genes in rod and cone photoreceptors. There may be another possibility that mr-s is involved in cell fate determination of rod photoreceptors versus cone photoreceptors. While cone photoreceptors are born during the early embryonic stages of mouse retinogenesis, rod photoreceptors are born primarily in the late embryonic and early postnatal period [48]. The expression pattern of mr-s may suggest that mr-s is expressed in rod photoreceptors but not in cone photoreceptors as well as Nr2e3, which is known as a transcriptional repressor and is thought to down-regulate cone photoreceptor-specific genes. To clarify the biological function of mr-s, analysis of mice with targeted disruptions of mr-s will be very important."}

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the present study, we identified a novel gene, mr-s, which is predominantly expressed in retinal photoreceptors and the pineal gland. The peak of mr-s expression in the developing retina is around P6. This expression pattern correlates with the rapid increase of Crx, rhodopsin and other photoreceptor genes around P6-P8. Around P6, the outer plexiform layer becomes visible and the outer layer of retina separates into two layers, ONL and INL. At the same time, photoreceptors begin to undergo terminal differentiation, forming the outer segment. We therefore hypothesized that mr-s is a key molecule in the late development of photoreceptors.\nWe previously reported that Otx2 and Crx have a critical role in photoreceptor development and that Otx2 directly regulates Crx transcription [3,9]. In situ hybridization and RT-PCR showed significant reduction of mr-s signal in the Crx KO retina and pineal gland. Furthermore, the luciferase assay demonstrated that Otx2 and Crx may directly upregulate the transcription of mr-s in mammalian cells. In retinal photoreceptor cells, the Otx2 transcripts are not highly expressed at P6-P9, while the Crx transcripts are strongly detected around P6. Therefore, our results strongly suggest that mr-s transcription is directly regulated by Crx. In the present study, Nrl, a photoreceptor-specific transcription factor that is highly expressed in photoreceptors at the postnatal stage, did not affect the transcription of mr-s. This finding is actually consistent with the analysis of the Nrl KO mouse which was recently reported [40]. The expression profiles of wild-type and Nrl KO retinas at P2, P10 and 2 months were analyzed and mr-s was not included in 161 differentially expressed genes in the Nrl KO retina.\nPrevious reports suggested that the SAM domain is a protein-protein interaction module. The SAM domain of the mr-s protein is closely related to that of ph and TEL, whose SAM domains can form a helical, head-to-tail polymeric structure and mediate the formation of a higher order chromatin structure. To characterize the biochemical function of mr-s, we performed yeast two-hybrid screening using full-length mr-s as the bait. As a result, the most frequent positive clones (5/28) in the screening were the cDNA fragments containing the SAM domain of mr-s. This strongly suggests that mr-s self-associates through its SAM domain. An immunoprecipitation assay, using two site-directed mutants of the SAM domain of mr-s, demonstrated that the mr-s protein can self-associate through its SAM domain in mammalian cells. While we did not address the question whether the SAM domain of mr-s forms a polymeric structure in the present study, the phylogenetic analysis of SAM domain of mr-s and other SAM domain-containing molecules suggests that mr-s can form head-to-tail polymer and mediate gene silencing by spreading repressive complexes along the chromatin similar to ph and/or TEL. Although our results in the immunoprecipitation assay demonstrated that the N-terminal constructs lacking a SAM domain still interact with each other, these results do not fit into the head-to-tail polymer model. We cannot exclude the possibility that the resulting protein-protein interaction of mr-s is an artifact of the overexpression conditions. The issue of whether or not mr-s forms a polymer awaits future analysis.\nA previous report indicated that TEL contains a sequence-specific DNA binding domain, namely the ETS domain, and binds to specific sites via its ETS domain [41]. TEL could serve to nucleate a polymer, which would spread by oligomerization of the SAM domain. In contrast to TEL, ph does not contain an obvious sequence-specific DNA binding motif (16). Therefore, its initial binding to the template may require protein-protein interactions with other sequence-specific transcriptional repressors. The segmentation gene-encoding transcriptional repressors such as Hunchback have a role in recruiting SAM domain-containing PcG proteins, which can spread along the template via polymerization [42]. Since mr-s does not contain obvious DNA binding motifs, we suppose that there is a sequence-specific transcription factor(s) which interacts with mr-s. However, we did not find any transcription factors in the present yeast two-hybrid screening.\nWe also found that full-length mr-s fused to the GAL4 DNA binding domain (DBD-mrs) functions as a transcriptional repressor. This may support the idea that mr-s is involved in repressive complexes similar to other SAM domain-containing proteins. Our results, however, showed that the self-association of mr-s through its SAM domain is not essential for the transcriptional repressive activity. Polymerization of the SAM domain has been previously reported to be essential for the repressive functions of ph and TEL [43,44]. On the other hand, human lethal(3) malignant brain tumor (H-L(3)MBT) protein, which also contains a SAM domain at the C-terminus, was reported as a transcriptional repressor and the repressor activity of H-L(3)MBT required mainly the presence of the MBT repeats but not the SAM domain [45]. To determine the transcriptional repressor region of the mr-s protein, we performed a luciferase assay using site-directed mutants (DBD-W404A and DBD-G453A). The result showed that the reduced binding ability of self-association partially compromises the transcriptional repressive activity of mr-s (Fig. 7D). However, the repressive effect was more significant when DBD-tail, which does not contain SAM domain, was co-introduced with the 5xGAL4-pGL3 reporter plasmid. Therefore, we conclude that a region from amino acids 463 to 542 is mainly responsible for the repressor activity in the case of mr-s. Evolutionary conservation of the C-terminal 80 aa region of mr-s from zebrafish through human may underlie the functional importance of this region.\nTwo distinct multiprotein PcG complexes, PRC1 and PRC2, have been identified. PRC2 is involved in the initiation of silencing and contains histone deacetylases (HDACs) and histone methyltransferases, which can methylate histone H3 lysine 9 and 27, marks of silenced chromatin. PRC1, including ph, recognizes the histone H3 lysine 27 mark set by PRC2 and maintains a stable state of gene repression in which PRC1 blocks chromatin remodeling by the trithorax group-related SWI-SNF complex [46,47]. Therefore, the mechanism of repression by PRC2 is thought to be HDAC-dependent while the mechanism of repression by PRC1 appears to be HDAC-independent. Our luciferase assay also showed that transcriptional repression of DBD-mrs was not affected by the addition of various concentrations of trichostatin A, a potent HDAC inhibitor (data not shown). Therefore, we speculate that the mechanism of repression of mr-s may be HDAC-independent and more similar to that of PRC1 complex.\nIn the present study, the biochemical experiments demonstrate that the mr-s protein functions as a transcriptional repressor and possibly down-regulates the spatial and temporal expression of the target genes during retinal photoreceptor development. Our data also revealed that the repressive activity of mr-s is mainly due to the C-terminal region (amino acids 463 to 542). However, downstream targets of mr-s still remain unclear. In situ hybridization showed that the peak of mr-s expression is around P6, when retinal photoreceptors undergo terminal differentiation. We hypothesize that the target genes of mr-s might be non-photoreceptor genes. In this case, mr-s may suppress the expression of non-photoreceptor genes in rod and cone photoreceptors. There may be another possibility that mr-s is involved in cell fate determination of rod photoreceptors versus cone photoreceptors. While cone photoreceptors are born during the early embryonic stages of mouse retinogenesis, rod photoreceptors are born primarily in the late embryonic and early postnatal period [48]. The expression pattern of mr-s may suggest that mr-s is expressed in rod photoreceptors but not in cone photoreceptors as well as Nr2e3, which is known as a transcriptional repressor and is thought to down-regulate cone photoreceptor-specific genes. To clarify the biological function of mr-s, analysis of mice with targeted disruptions of mr-s will be very important."}