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.
|Number of pages||4|
|State||Published - May 10 2016|
Bibliographical noteFunding Information:
This work was supported by the National Science Foundation (MCB 1158036, Y.W.) and National Institute of Allergy and Infectious Diseases (1R21AI103717, Y.W.; R01 AI051517, R.E.D.; and F31 fellowship AI120653-01, S.R.W.).
© 2016 American Chemical Society.
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