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PMID: 3536487 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The C terminus of penicillin-binding protein 5 is essential for localisation to the E. coli inner membrane.

The EMBO journal ·Vol. 5 ·No. 9 ·1986-09-00 ·Pages 2399-405

Pratt JM, Jackson ME, Holland IB

Abstract

Penicillin-binding protein 5 (PBP5) has been previously identified as a component of the inner membrane of Escherichia coli and we present here further evidence that PBP5 is tightly bound to the membrane. To investigate the regions of PBP5 involved in membrane binding we have constructed a series of C-terminal deletions and shown that the removal of as few as 10 amino acids results in the release of the truncated protein into the periplasm. The C terminus, therefore, appears to be important for interaction with the membrane; however, inspection of the amino acid sequence does not reveal extended runs of hydrophobicity typical of a membrane anchor. Thus we conclude that PBP5 is anchored to the inner membrane by a mechanism not previously described.

MeSH Terms
Amino Acid Sequence Bacterial Proteins Binding Sites Carrier Proteins/genetics,metabolism Cell Membrane/metabolism Chromosome Deletion Escherichia coli/metabolism Genes Genes, Bacterial Genotype Hexosyltransferases Muramoylpentapeptide Carboxypeptidase/genetics,metabolism Penicillin-Binding Proteins Peptidyl Transferases Plasmids Protein Binding
Chemicals
Bacterial Proteins Carrier Proteins Penicillin-Binding Proteins Peptidyl Transferases Hexosyltransferases Muramoylpentapeptide Carboxypeptidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pratt J M
Jackson M E
Holland I B
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34 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1986-09-00
Pages
2399-405
Language
English
Region
England
NLM ID
8208664
PMCID
PMC1167126
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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