The ssrA-Tag Facilitated Degradation of an Integral Membrane Protein

Qian Chai, Zhaoshuai Wang, Stacy R. Webb, Rebecca E. Dutch, Yinan Wei

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

ATP-dependent degradation plays a critical role in the quality control and recycling of proteins in cells. However, complete degradation of membrane proteins by ATP-dependent proteases in bacteria is not well-studied. We discovered that the degradation of a multidomain and multispan integral membrane protein AcrB could be facilitated by the introduction of a ssrA-tag at the C-terminus of the protein sequence and demonstrated that the cytoplasmic unfoldase-protease complex ClpXP was involved in the degradation. This is the first report to our knowledge to reveal that the ClpXP complex is capable of degrading integral membrane proteins. The chaperone SspB also played a role in the degradation. Using purified proteins, we demonstrated that the addition of the ssrA-tag did not drastically affect the structure of AcrB, and the degradation of detergent solubilized AcrB by purified ClpXP could be observed in vitro.

Original languageEnglish
Pages (from-to)2301-2304
Number of pages4
JournalBiochemistry
Volume55
Issue number16
DOIs
StatePublished - May 10 2016

Bibliographical note

Publisher Copyright:
© 2016 American Chemical Society.

ASJC Scopus subject areas

  • Biochemistry

Fingerprint

Dive into the research topics of 'The ssrA-Tag Facilitated Degradation of an Integral Membrane Protein'. Together they form a unique fingerprint.

Cite this