RRC ID 3207
Author Kanehara K, Ito K, Akiyama Y.
Title YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA.
Journal EMBO J.
Abstract sigmaE is an alternative sigma factor involved in a pathway of extracytoplasmic stress responses in Escherichia coli. Under normal growth conditions, sigmaE activity is down-regulated by the membrane-bound anti-sigmaE protein, RseA. Extracytoplasmic stress signals induce degradation of RseA by two successive proteolytic events: DegS-catalyzed first cleavage at a periplasmic site followed by YaeL-mediated second proteolysis at an intramembrane region. Normally, the second reaction (site-2 proteolysis) only occurs after the first cleavage (site-1 cleavage). Here, we show that YaeL variants with the periplasmic PDZ domain deleted or mutated allows unregulated cleavage of RseA and consequent sigmaE activation. It was also found that a glutamine-rich region in the periplasmic domain of RseA was required for the avoidance of the YaeL-mediated proteolysis in the absence of site-1 cleavage. These results indicate that multiple negative elements both in the enzyme (PDZ domain) and in the substrate (glutamine-rich region) determine the strict dependence of the site-2 proteolysis on the site-1 cleavage.
Volume 22(23)
Pages 6389-98
Published 2003-12-1
DOI 10.1093/emboj/cdg602
PMID 14633997
PMC PMC291843
MeSH Amino Acid Sequence Binding Sites Endopeptidases / chemistry* Endopeptidases / metabolism* Escherichia coli Proteins / chemistry* Escherichia coli Proteins / metabolism* Genetic Complementation Test Glutamine* Kinetics Membrane Proteins / chemistry* Membrane Proteins / metabolism* Molecular Sequence Data Mutagenesis Plasmids Recombinant Proteins / chemistry Recombinant Proteins / metabolism Sequence Alignment Sequence Homology, Amino Acid Transcription Factors / chemistry* Transcription Factors / metabolism*
IF 10.557
Times Cited 76
Prokaryotes E. coli ?