2011 Fiscal Year Final Research Report
Mechanisms of oxidative protein folding in the periplasm of E. coli
Project/Area Number |
21580092
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied microbiology
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Research Institution | Nara Institute of Science and Technology |
Principal Investigator |
KADOKURA Hiroshi 奈良先端科学技術大学院大学, バイオサイエンス研究科, 研究員 (70224558)
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Project Period (FY) |
2009 – 2011
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Keywords | ジスルフィド結合 / 立体構造形成 / 分泌 / DsbA |
Research Abstract |
Disulfide bonds, formed between pairs of cysteines, are important for the folding,activity, and stability of many secretory and membrane proteins. In a bacterium Escherichia coli, an enzyme called DsbA introduces disulfide bonds into folding proteins in the periplasm. In this study, I detected, in vivo, the intermediates of disulfide bond formation that were formed between DsbA and its substrates. Detailed characterization of the intermediates revealed a number of new insights into protein folding in this cellular compartment.
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[Journal Article] rearrangement triggered by translocon assembly controls lipopolysaccharide export2012
Author(s)
Chng, S.S., Xue, M., Garner, R.A.,Kadokura, H., Boyd, D., Beckwith, J.,Kahne, D. Disulfide
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Journal Title
Science
Volume: 337
Pages: 1665-1668
Peer Reviewed
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