Elucidation of the working principle of repetitive motors driving protein export

2016 Fiscal Year Final Research Report

• Project Area: Harmonized supramolecular machinery for motility and its diversity
• Project/Area Number: 24117003
• Research Category: Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
• Allocation Type: Single-year Grants
• Review Section: Biological Sciences
• Research Institution: Kyoto University
• Principal Investigator: Mori Hiroyuki 京都大学, ウイルス・再生医科学研究所, 准教授 (10243271)
• Co-Investigator(Renkei-kenkyūsha): TSUKAZAKI Tomoya 奈良先端科学技術大学院大学, バイサイエンス研究科, 准教授 (80436716)
• Project Period (FY): 2012-06-28 – 2017-03-31
• Keywords: SecDF / タンパク質膜透過 / プロトン駆動力 / SecA ATPase / 大腸菌 / ビブリオ菌

Outline of Final Research Achievements

In bacteria, protein translocation is mediated by two repetitive motors, SecA ATPase and SecDF, which exist on the cytoplasmic side and periplasic side of the SecYEG channel, respectively. In order to elucidate how these two motors contribute to protein translocation reaction, we carried out the following experiments. 1) We systematically performed site-directed in vivo photo cross-linking experiments targeted to E. coli SecD and identified a substrate binding site in the SecD protein. 2) We determined new crystal structures of SecDF in collaboration with Dr. Tsukazaki and carried out structure-instructed biochemical studies.　3) We determined biochemical properties and physiological functions of two SecDF paralogs in Vibrio alginolyticus.

Free Research Field

生化学