大阪大学 · 生化学・遺伝学・分子生物学
Shinohara教授の研究室は、DNA二重鎖切断の修復と染色体の分配を制御する分子機構に焦点を当てており、特にRad52とRad51を介した遺伝子再結合のメカニズムや、ミトーシスとミーオシスにおける再結合酵素の機能的役割を解明しています。特に、RPAと協働するRad52による単鎖DNAのアンナリング機構や、Dmc1とRad51の協調的働きが染色体の交差形成に与える影響を分子細胞生物学的手法で解明しています。また、染色体凝縮酵素とPolo様キナーゼがセパラーゼ非依存的にコhesinを染色体から放出するという新規な調節機構の解明にも貢献しています。
Figures are computed from collected data and may differ slightly.
Rad52 forms a ring-like structure and binds to ssDNA. Its structure and DNA binding properties are different from those of Rad51. The interaction of Rad52 with RPA plays an important role in the enhancement of annealing of complementary ssDNAs. We therefore propose that Rad52 mediates the RAD51-independent recombination through an ssDNA annealing, assisted by RPA.
RecA protein is involved in homology search and strand exchange processes during recombination. Mitotic cells in eukaryotes express one RecA, Rad51, which is essential for the repair of double-strand breaks (DSBs). Additionally, meiotic cells induce the second RecA, Dmc1. Both Rad51 and Dmc1 are necessary to generate a crossover between homologous chromosomes, which ensures the segregation of the chromosomes at meiotic division I. It is largely unknown how the two RecAs cooperate during meiotic
Sister chromatid cohesion on chromosome arms is essential for the segregation of homologous chromosomes during meiosis I while it is dispensable for sister chromatid separation during mitosis. It was assumed that, unlike the situation in mitosis, chromosome arms retain cohesion prior to onset of anaphase-I. Paradoxically, reduced immunostaining signals of meiosis-specific cohesin, including the kleisin Rec8, were observed on chromosomes during late prophase-I of budding yeast. This decrease is s
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