| Project/Area Number |
18570188
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | University of Tsukuba |
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Principal Investigator |
KIMURA Keiji University of Tsukuba, Graduate School of Life and Environmental Sciences, Associate Professor (50332268)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,110,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥510,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2006: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | condensin / SMC / chromatin / mitotic chromosomes / ATP / 染色体凝縮 / SMCタンパク質 / 細胞周期 / クロマチン構造 |
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| Research Abstract |
Condensin is a conserved five-subunit protein complex composed of SMC heterodimer (SMC2/CAP-E and SMC4/CAP-C) and three other non-SMC subunits, and plays an essential role in mitotic chromosome condensation. Recently, it is reported that condensin is implicated in chromatin regulation during interphase, such as DNA repair, damage checkpoint response and transcriptional regulation. Purified condensin has an activity to introduce positive supercoiles into DNA in the presence of ATP. In higher eukaryotes, two condensin isoform, condensin I and condensin II are expressed.
Condensin I is phosphorylated by CK2 during interphase in addition to the mitotic phosphorylation by Cdc2. In contrast to the stimulatory effect of Cdc2-mediated phosphorylation during mitosis, phosphorylation by CK2 reduced the supercoiling activity of condensin I. CK2-mediated phosphorylation of condensin I is spatially and temporally regulated in a manner different to that of Cdc2-mediated phosphorylation: CK2-dependent phosphorylation during Interphase and decreases on chromosomes during mitosis. These finding is the first demonstration of a negative regulatory mode of condensin I.
It is also found that PP2A is required for the chromosomal association of condensin II. Interestingly, phosphatase activity of PP2A is not required for chromosomal association of condensin II. PP2A works as a chaperon that brings and localizes condensin II to chromosomes.
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