Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli sigma(32) by lambdaCIII

The FEBS Journal
Sabyasachi HalderPradeep Parrack

Abstract

The CIII protein of bacteriophage lambda exhibits antiproteolytic activity against the ubiquitous metalloprotease HflB (FtsH) of Escherichia coli, thereby stabilizing the lambdaCII protein and promoting lysogenic development of the phage. CIII also protects E.coli sigma(32), another substrate of HflB. We have recently shown that the protection of CII from HflB by CIII involves direct CIII-HflB binding, without any interaction between CII and CIII [HalderS, DattaAB & Parrack P (2007) J Bacteriol189, 8130-8138]. Such a mode of action for lambdaCIII would be independent of the HflB substrate. In this study, we tested the ability of CIII to protect sigma(32) from HflB digestion. The inhibition of HflB-mediated proteolysis of sigma(32) by CIII is very similar to that of lambdaCII, characterized by an enhanced protection by the core CIII peptide CIIIC (amino acids 14-41 of lambdaCIII) and a lack of interaction between sigma(32) and CIII.

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Citations

Mar 13, 2014·Annual Review of Biochemistry·Gisela StorzKumaran S Ramamurthi
Apr 7, 2016·Theory in Biosciences = Theorie in Den Biowissenschaften·Surama Biswas, Sriyankar Acharyya
May 18, 2017·Proceedings of the National Academy of Sciences of the United States of America·Hanbo WangGisela Storz

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