Ribosomal stalk complex driving translation cycle: molecular basis for high-speed and high-efficiency

2014 Fiscal Year Final Research Report

• Project/Area Number: 24370073
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Molecular biology
• Research Institution: Niigata University
• Principal Investigator: UCHIUMI Toshio 新潟大学, 自然科学系, 教授 (50143764)
• Co-Investigator(Kenkyū-buntansha): ITO Kosuke 新潟大学, 自然科学系, 助教 (20502397) ; YAO Minn 北海道大学, 大学院先端生命科学研究院, 教授 (40311518) ; MIYOSHI Tomohiro 新潟大学, 研究推進機構, 助教 (60534550) ; UCHIYAMA Susumu 大阪大学, 工学研究科, 准教授 (90335381)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: リボソーム / 翻訳因子 / リボソームストーク / リボソームタンパク質 / 遺伝情報翻訳 / EF-1α / EF-2 / IF5B

Outline of Final Research Achievements

We have studied on the ribosomal stalk protein complex, which determines the rate and efficiency of protein synthesis (translation), by using biochemical and crystallographic approaches, as follows: 1) multiple copies of the stalk proteins all bind to the ribosomal core via their N-terminal domains, and the C-terminal region of each stalk is flexible and moving widely around the ribosome; 2) the crystal structural data indicate that the C-terminal region of the stalk protein binds to individual translation factors through hydrophobic interactions; 3) the interactions between the C-terminal region of the stalk protein and translation factors is important to recruit the factors to the functional center within the ribosomal core. These lines of evidence demonstrate the crucial contribution of the stalk protein to efficient translation.

Free Research Field

分子生物学