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101.
When cells exit from mitotic cell division, their sister chromatids lose cohesion and separate to opposite poles of the dividing cell, resulting in equational chromosome segregation. In contrast, the reductional segregation of the first stage of meiotic cell division (meiosis I) requires that sister chromatids remain associated through their centromeres and move together to the same pole. Centromeric cohesion is lost as cells exit from meiosis II and sister chromatids can then separate. The fission yeast cohesin protein Rec8 is specific to and required for meiosis. Here we show that Rec8 appears in the centromeres and adjacent chromosome arms during the pre-meiotic S phase. Centromeric Rec8 persists throughout meiosis I and disappears at anaphase of meiosis II. When the rec8 gene is deleted, sister chromatids separate at meiosis I, resulting in equational rather than reductional chromosome segregation. We propose that the persistence of Rec8 at centromeres during meiosis I maintains sister-chromatid cohesion, and that its presence in the centromere-adjacent regions orients the kinetochores so that sister chromatids move to the same pole. This results in the reductional pattern of chromosome segregation necessary to reduce a diploid zygote to haploid gametes. 相似文献
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J. Sasaki M. Imanaka S. Watanabe N. Otsuka K. Sugiyama 《Cellular and molecular life sciences : CMLS》1982,38(4):495-496
Summary Rabbit anti-rat plasma fibronectin (pFN) causes histamine release from rat mast cells in the presence of complement. Fibronectin (FN) on rat mast cells, as shown by immuno-electron microscopy, is principally localized on cell folds, so they may play a role of attachment in the matrix of connective tissue.Acknowledgment. This work is supported by grants (No. 56770014 and No. 544018) from the Ministry of Education, Science and Culture of Japan. 相似文献
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Sex chromatin of unstained mouse amniotic cells was identifiable using ordinary brightfield microscopy with optimal setting of the illumination. 相似文献
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K. Morita S. Inoue Y. Murai K. Watanabe S. Shima 《Cellular and molecular life sciences : CMLS》1982,38(10):1227-1228
Summary Cap formation in mouse spleen cells induced by antiimmunoglobulin was inhibited by the metals Be, Fe, Cu and Al. Be was especially strong as an inhibitor of cap formation. It is suggested that these metals might change the mobility of the membrane and have some biological effects on the cross association of antigen receptors when B lymphocytes are attached by them. 相似文献
108.
The centromere of a chromosome is composed mainly of two domains, a kinetochore assembling core centromere and peri-centromeric heterochromatin regions. The crucial role of centromeric heterochromatin is still unknown, because even in simpler unicellular organisms such as the fission yeast Schizosaccharomyces pombe, the heterochromatin protein Swi6 (HP1 homologue) has several functions at centromeres, including silencing gene expression and recombination, enriching cohesin, promoting kinetochore assembly, and, ultimately, preventing erroneous microtubule attachment to the kinetochores. Here we show that the requirement of heterochromatin for mitotic chromosome segregation is largely replaced by forcibly enriching cohesin at centromeres in fission yeast. However, this enrichment of cohesin is not sufficient to replace the meiotic requirement for heterochromatin. We find that the heterochromatin protein Swi6 associates directly with meiosis-specific shugoshin Sgo1, a protector of cohesin at centromeres. A point mutation of Sgo1 (V242E), which abolishes the interaction with Swi6, impairs the centromeric localization and function of Sgo1. The forced centromeric localization of Sgo1 restores proper meiotic chromosome segregation in swi6 cells. We also show that the direct link between HP1 and shugoshin is conserved in human cells. Taken together, our findings suggest that the recruitment of shugoshin is the important primary role for centromeric heterochromatin in ensuring eukaryotic chromosome segregation. 相似文献
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In vitro synthesized bacterial outer membrane protein is integrated into bacterial inner membranes but translocated across microsomal membranes 总被引:7,自引:0,他引:7
The LamB protein is an integral membrane protein of the outer membrane of Escherichia coli. We have now found that, when synthesized in an E. coli cell-free translation system supplemented with inverted vesicles derived from the E. coli inner membrane, LamB protein is integrated into the vesicle membrane as assayed by its resistance to extraction at alkaline pH. These data suggest that the inner membrane is the primary site for integration of LamB protein prior to subsequent sorting to the outer membrane. When synthesized in a wheat germ cell-free translation system supplemented with canine microsomal membranes, LamB protein is glycosylated at one or two cryptic sites, and surprisingly, it is translocated across instead of being integrated into the vesicle membrane. We suggest that the translocation machinery of the microsomal membrane, although able to recognize the signal sequence(s) of LamB, is unable to recognize its stop-transfer sequence(s), thereby yielding translocation instead of integration. 相似文献