PMC:509301 / 24924-27882 JSONTXT

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in Punctate Nuclear Foci Is Developmentally Regulated\nIn order to examine the subcellular distribution of Tif1γ protein, we generated an affinity-purified rabbit polyclonal antiserum directed against the C-terminal 15 amino acids conserved in human TIF1γ and mouse Tif1γ. Immunofluorescence of mouse embryo fibroblast nuclei with the anti-Tif1γ antiserum demonstrates that Tif1γ is localized in small nuclear foci (Figure 6A). The localization of Tif1γ protein appears different from the more diffuse nuclear patterns typically seen in studies of Tif1α (Remboutsika et al. 2002) or TIF1β (Cammas et al. 2002). A recent report demonstrates that TIF1β associates with heterochromatin-containing foci after retinoic acid treatment or serum starvation (Cammas et al. 2002). Thus, localization or expression of the TIF1 proteins may be regulated during distinct developmental processes or by environmental cues. The nuclear foci that contain Tif1γ do not colocalize with two markers of heterochromatin, HP1α protein and DAPI staining of DNA (Figure 6A). Furthermore, Tif1γ does not colocalize with promyelocytic leukemia gene product (PML) nuclear bodies, DNA repair complexes that contain Mre11, or transcriptional complexes containing TFII-B (unpublished data). We next examined the expression of Tif1γ protein during the differentiation of G1E cells, a murine erythroleukemia cell line that can terminally differentiate into erythrocytes when a Gata1:estrogen receptor fusion protein is stabilized in response to estrogen exposure (Weiss et al. 1997). Western blot analysis demonstrated that Tif1γ protein expression decreases with terminal erythroid differentiation (Figure 6B). Consistent with this finding, after 24 hpf, zebrafish mon mRNA expression falls during the terminal maturation of the primitive erythroid cells (unpublished data). In two different murine erythroleukemia cell lines (MEL and G1E), Tif1γ is also expressed in nuclear foci, and even though the overall Tif1γ protein level is reduced, this nuclear foci localization does not change with differentiation (unpublished data). This provides further support for the hypothesis that Tif1γ acts within novel nuclear foci, during erythroid differentiation.\nFigure 6 Mammalian Tif1γ Protein Localizes to Nuclear Bodies Distinct from Heterochromatin\n(A) Deconvolved immunofluorescence images of a mouse embryonic fibroblast cell nucleus stained with an anti-Tif1γ antibody and stained with a monoclonal antibody directed against HP1α. This is also compared to DAPI staining. The merged images of the nucleus show that Tif1γ does not colocalize with the HP1α or DAPI staining of heterochromatin while HP1α and DAPI staining overlap.\n(B) G1ER mouse erythroleukemia cells express high levels of Tif1γ protein as detected by Western blot analysis. Expression of Tif1γ decreases during Gata1-dependent erythroid maturation induced by β-estradiol treatment to induce a Gata1–ER fusion protein."}

{"project":"2_test","denotations":[{"id":"15314655-12384511-84850904","span":{"begin":579,"end":583},"obj":"12384511"},{"id":"15314655-12154074-84850905","span":{"begin":609,"end":613},"obj":"12154074"},{"id":"15314655-12154074-84850906","span":{"begin":769,"end":773},"obj":"12154074"},{"id":"15314655-9032291-84850907","span":{"begin":1549,"end":1553},"obj":"9032291"},{"id":"T8286","span":{"begin":579,"end":583},"obj":"12384511"},{"id":"T38592","span":{"begin":609,"end":613},"obj":"12154074"},{"id":"T35680","span":{"begin":769,"end":773},"obj":"12154074"},{"id":"T13610","span":{"begin":1549,"end":1553},"obj":"9032291"}],"text":"Tif1γ in Punctate Nuclear Foci Is Developmentally Regulated\nIn order to examine the subcellular distribution of Tif1γ protein, we generated an affinity-purified rabbit polyclonal antiserum directed against the C-terminal 15 amino acids conserved in human TIF1γ and mouse Tif1γ. Immunofluorescence of mouse embryo fibroblast nuclei with the anti-Tif1γ antiserum demonstrates that Tif1γ is localized in small nuclear foci (Figure 6A). The localization of Tif1γ protein appears different from the more diffuse nuclear patterns typically seen in studies of Tif1α (Remboutsika et al. 2002) or TIF1β (Cammas et al. 2002). A recent report demonstrates that TIF1β associates with heterochromatin-containing foci after retinoic acid treatment or serum starvation (Cammas et al. 2002). Thus, localization or expression of the TIF1 proteins may be regulated during distinct developmental processes or by environmental cues. The nuclear foci that contain Tif1γ do not colocalize with two markers of heterochromatin, HP1α protein and DAPI staining of DNA (Figure 6A). Furthermore, Tif1γ does not colocalize with promyelocytic leukemia gene product (PML) nuclear bodies, DNA repair complexes that contain Mre11, or transcriptional complexes containing TFII-B (unpublished data). We next examined the expression of Tif1γ protein during the differentiation of G1E cells, a murine erythroleukemia cell line that can terminally differentiate into erythrocytes when a Gata1:estrogen receptor fusion protein is stabilized in response to estrogen exposure (Weiss et al. 1997). Western blot analysis demonstrated that Tif1γ protein expression decreases with terminal erythroid differentiation (Figure 6B). Consistent with this finding, after 24 hpf, zebrafish mon mRNA expression falls during the terminal maturation of the primitive erythroid cells (unpublished data). In two different murine erythroleukemia cell lines (MEL and G1E), Tif1γ is also expressed in nuclear foci, and even though the overall Tif1γ protein level is reduced, this nuclear foci localization does not change with differentiation (unpublished data). This provides further support for the hypothesis that Tif1γ acts within novel nuclear foci, during erythroid differentiation.\nFigure 6 Mammalian Tif1γ Protein Localizes to Nuclear Bodies Distinct from Heterochromatin\n(A) Deconvolved immunofluorescence images of a mouse embryonic fibroblast cell nucleus stained with an anti-Tif1γ antibody and stained with a monoclonal antibody directed against HP1α. This is also compared to DAPI staining. The merged images of the nucleus show that Tif1γ does not colocalize with the HP1α or DAPI staining of heterochromatin while HP1α and DAPI staining overlap.\n(B) G1ER mouse erythroleukemia cells express high levels of Tif1γ protein as detected by Western blot analysis. Expression of Tif1γ decreases during Gata1-dependent erythroid maturation induced by β-estradiol treatment to induce a Gata1–ER fusion protein."}

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in Punctate Nuclear Foci Is Developmentally Regulated\nIn order to examine the subcellular distribution of Tif1γ protein, we generated an affinity-purified rabbit polyclonal antiserum directed against the C-terminal 15 amino acids conserved in human TIF1γ and mouse Tif1γ. Immunofluorescence of mouse embryo fibroblast nuclei with the anti-Tif1γ antiserum demonstrates that Tif1γ is localized in small nuclear foci (Figure 6A). The localization of Tif1γ protein appears different from the more diffuse nuclear patterns typically seen in studies of Tif1α (Remboutsika et al. 2002) or TIF1β (Cammas et al. 2002). A recent report demonstrates that TIF1β associates with heterochromatin-containing foci after retinoic acid treatment or serum starvation (Cammas et al. 2002). Thus, localization or expression of the TIF1 proteins may be regulated during distinct developmental processes or by environmental cues. The nuclear foci that contain Tif1γ do not colocalize with two markers of heterochromatin, HP1α protein and DAPI staining of DNA (Figure 6A). Furthermore, Tif1γ does not colocalize with promyelocytic leukemia gene product (PML) nuclear bodies, DNA repair complexes that contain Mre11, or transcriptional complexes containing TFII-B (unpublished data). We next examined the expression of Tif1γ protein during the differentiation of G1E cells, a murine erythroleukemia cell line that can terminally differentiate into erythrocytes when a Gata1:estrogen receptor fusion protein is stabilized in response to estrogen exposure (Weiss et al. 1997). Western blot analysis demonstrated that Tif1γ protein expression decreases with terminal erythroid differentiation (Figure 6B). Consistent with this finding, after 24 hpf, zebrafish mon mRNA expression falls during the terminal maturation of the primitive erythroid cells (unpublished data). In two different murine erythroleukemia cell lines (MEL and G1E), Tif1γ is also expressed in nuclear foci, and even though the overall Tif1γ protein level is reduced, this nuclear foci localization does not change with differentiation (unpublished data). 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in Punctate Nuclear Foci Is Developmentally Regulated\nIn order to examine the subcellular distribution of Tif1γ protein, we generated an affinity-purified rabbit polyclonal antiserum directed against the C-terminal 15 amino acids conserved in human TIF1γ and mouse Tif1γ. Immunofluorescence of mouse embryo fibroblast nuclei with the anti-Tif1γ antiserum demonstrates that Tif1γ is localized in small nuclear foci (Figure 6A). The localization of Tif1γ protein appears different from the more diffuse nuclear patterns typically seen in studies of Tif1α (Remboutsika et al. 2002) or TIF1β (Cammas et al. 2002). A recent report demonstrates that TIF1β associates with heterochromatin-containing foci after retinoic acid treatment or serum starvation (Cammas et al. 2002). Thus, localization or expression of the TIF1 proteins may be regulated during distinct developmental processes or by environmental cues. The nuclear foci that contain Tif1γ do not colocalize with two markers of heterochromatin, HP1α protein and DAPI staining of DNA (Figure 6A). Furthermore, Tif1γ does not colocalize with promyelocytic leukemia gene product (PML) nuclear bodies, DNA repair complexes that contain Mre11, or transcriptional complexes containing TFII-B (unpublished data). We next examined the expression of Tif1γ protein during the differentiation of G1E cells, a murine erythroleukemia cell line that can terminally differentiate into erythrocytes when a Gata1:estrogen receptor fusion protein is stabilized in response to estrogen exposure (Weiss et al. 1997). Western blot analysis demonstrated that Tif1γ protein expression decreases with terminal erythroid differentiation (Figure 6B). Consistent with this finding, after 24 hpf, zebrafish mon mRNA expression falls during the terminal maturation of the primitive erythroid cells (unpublished data). In two different murine erythroleukemia cell lines (MEL and G1E), Tif1γ is also expressed in nuclear foci, and even though the overall Tif1γ protein level is reduced, this nuclear foci localization does not change with differentiation (unpublished data). This provides further support for the hypothesis that Tif1γ acts within novel nuclear foci, during erythroid differentiation.\nFigure 6 Mammalian Tif1γ Protein Localizes to Nuclear Bodies Distinct from Heterochromatin\n(A) Deconvolved immunofluorescence images of a mouse embryonic fibroblast cell nucleus stained with an anti-Tif1γ antibody and stained with a monoclonal antibody directed against HP1α. This is also compared to DAPI staining. The merged images of the nucleus show that Tif1γ does not colocalize with the HP1α or DAPI staining of heterochromatin while HP1α and DAPI staining overlap.\n(B) G1ER mouse erythroleukemia cells express high levels of Tif1γ protein as detected by Western blot analysis. Expression of Tif1γ decreases during Gata1-dependent erythroid maturation induced by β-estradiol treatment to induce a Gata1–ER fusion protein."}