2011 Fiscal Year Final Research Report
Study of ribosome maturation mechanism by the structural analysis of Rat-U13snoRNA complex
Project/Area Number |
20247007
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Research Category |
Grant-in-Aid for Scientific Research (A)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Hokkaido University |
Principal Investigator |
TANAKA Isao 北海道大学, 大学院・先端生命科学研究院, 特任教授 (70093052)
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Co-Investigator(Kenkyū-buntansha) |
YAO Min 北海道大学, 大学院・先端生命科学研究院, 教授 (40311518)
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Co-Investigator(Renkei-kenkyūsha) |
SUZUKI Tsutomu 東京大学, 大学院・工学系研究科, 教授 (20292782)
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Project Period (FY) |
2008 – 2011
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Keywords | X線結晶構造解析 / RNA-タンパク質相互作用 / snoRNA / リボソーム生合成 / アセチル化 |
Research Abstract |
Using the proteins from M.musculus (mRAT) and from S.cerevisiae RAT (yRAT), it has been directly proved that a eucaryotic homolog of E. coli tRNA acetyltransferase TmcA (RAT) has the activity of transferring the acetyl group to the specific site of 18S rRNA. It has also been proved that these proteins have the ATPase activity. As a result of crystallization screening, we found that the crystals of RAT from S.cerevisiae of which C-terminal 123 residues are truncated (deltaC123-yRAT) diffract X-rays to 9 A resolution at BL32XU, SPring-8.
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Research Products
(42 results)
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[Journal Article] Archaeal ribosomal stalk protein interacts with translation factors in a nucleotide-independent manner via its conserved C terminus, Proc.Natl2012
Author(s)
Nomura N, Honda T, Baba K, Naganuma T, Tanzawa T, Arisaka F, Noda M, Uchiyama S, Tanaka I, Yao M, Uchiumi T
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Journal Title
Acad. Sci. USA
Volume: 109
Pages: 3748-3753
DOI
Peer Reviewed
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