Allosteric activation of a bacterial stress sensor

Nieng Yan; Yigong Shi

doi:10.1016/j.cell.2007.10.021

Allosteric activation of a bacterial stress sensor

Cell. 2007 Nov 2;131(3):441-3. doi: 10.1016/j.cell.2007.10.021.

Authors

Nieng Yan¹, Yigong Shi

Affiliation

¹ Center for Structural Biology, Institute of Biomedicine, Tsinghua University, Beijing, China. structure@tsinghua.edu.cn

PMID: 17981109
DOI: 10.1016/j.cell.2007.10.021

Abstract

In Gram-negative bacteria, envelope stress signals such as unfolded outer membrane proteins (OMP) activate the periplasmic protease DegS. This protease then triggers a cellular pathway to alleviate the stress. Now Sohn et al. (2007) show conclusively that inhibition of DegS is relieved allosterically by binding of the C-terminal sequences in unfolded OMPs to the PDZ domain of DegS.

Publication types

Comment

MeSH terms

Allosteric Regulation
Bacterial Outer Membrane Proteins / chemistry
Bacterial Outer Membrane Proteins / metabolism
Enzyme Activation
Escherichia coli / enzymology*
Escherichia coli Proteins / antagonists & inhibitors
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / metabolism*
Membrane Proteins / metabolism
Mutant Proteins / chemistry
Mutant Proteins / metabolism
PDZ Domains
Peptides / chemistry
Peptides / metabolism
Protein Binding
Substrate Specificity
Transcription Factors / metabolism

Substances

Bacterial Outer Membrane Proteins
Escherichia coli Proteins
Membrane Proteins
Mutant Proteins
Peptides
RseA protein, E coli
Transcription Factors
degS protein, Escherichia coli