Insights into the function of YciM, a heat shock membrane protein required to maintain envelope integrity in Escherichia coli.

TitleInsights into the function of YciM, a heat shock membrane protein required to maintain envelope integrity in Escherichia coli.
Publication TypeJournal Article
Year of Publication2014
AuthorsNicolaes, V., H. El Hajjaji, R. M. Davis, C. Van der Henst, M. Depuydt, P. Leverrier, A. Aertsen, V. Haufroid, S. Ollagnier de Choudens, X. De Bolle, N. Ruiz, and J-F. Collet
JournalJ Bacteriol
Volume196
Issue2
Pagination300-9
Date Published2014 Jan
ISSN1098-5530
KeywordsAmino Acid Motifs, Amino Acid Sequence, Bacteriolysis, Cell Membrane, Culture Media, Endopeptidases, Escherichia coli, Escherichia coli Proteins, Gene Deletion, Hot Temperature, Iron, Membrane Proteins, Microscopy, Molecular Sequence Data, Osmotic Pressure, Protein Binding, Protein Interaction Mapping, Sequence Alignment
Abstract

The cell envelope of Gram-negative bacteria is an essential organelle that is important for cell shape and protection from toxic compounds. Proteins involved in envelope biogenesis are therefore attractive targets for the design of new antibacterial agents. In a search for new envelope assembly factors, we screened a collection of Escherichia coli deletion mutants for sensitivity to detergents and hydrophobic antibiotics, a phenotype indicative of defects in the cell envelope. Strains lacking yciM were among the most sensitive strains of the mutant collection. Further characterization of yciM mutants revealed that they display a thermosensitive growth defect on low-osmolarity medium and that they have a significantly altered cell morphology. At elevated temperatures, yciM mutants form bulges containing cytoplasmic material and subsequently lyse. We also discovered that yciM genetically interacts with envC, a gene encoding a regulator of the activity of peptidoglycan amidases. Altogether, these results indicate that YciM is required for envelope integrity. Biochemical characterization of the protein showed that YciM is anchored to the inner membrane via its N terminus, the rest of the protein being exposed to the cytoplasm. Two CXXC motifs are present at the C terminus of YciM and serve to coordinate a redox-sensitive iron center of the rubredoxin type. Both the N-terminal membrane anchor and the C-terminal iron center of YciM are important for function.

DOI10.1128/JB.00921-13
Alternate JournalJ. Bacteriol.
PubMed ID24187084
PubMed Central IDPMC3911248
Grant ListR01 GM100951 / GM / NIGMS NIH HHS / United States
R01GM100951 / GM / NIGMS NIH HHS / United States
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