Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control

Qing Tao Shen, Xiao Chen Bai, Lei Fu Chang, Yi Wu, Hong Wei Wang, Sen Fang Sui

Research output: Contribution to journalArticle

55 Scopus citations

Abstract

In the periplasm of Escherichia coli, DegP (also known as HtrA), which has both chaperone-like and proteolytic activities, prevents the accumulation of toxic misfolded and unfolded polypeptides. In solution, upon binding to denatured proteins, DegP forms large cage-like structures. Here, we show that DegP forms a range of bowl-shaped structures, independent of substrate proteins, each with a 4-, 5-, or 6-fold symmetry and all with a DegP trimer as the structural unit, on lipid membranes. These membrane-bound DegP assemblies have the capacity to recruit and process substrates in the bowl chamber, and they exhibit higher proteolytic and lower chaperone-like activities than DegP in solution. Our findings imply that DegP might regulate its dual roles during protein quality control, depending on its assembly state in the narrow bacterial envelope.

Original languageEnglish (US)
Pages (from-to)4858-4863
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number12
DOIs
StatePublished - Mar 24 2009

Keywords

  • Chaperone
  • Cryo-electron microscopy
  • HtrA
  • Protease

ASJC Scopus subject areas

  • General

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