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Analysis of the membrane‐binding domain of penicillin‐binding protein 5 of Escherichia coli
Author(s) -
Jackson M. E.,
Pratt J. M.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00064.x
Subject(s) - periplasmic space , biology , penicillin binding proteins , escherichia coli , amphiphile , biochemistry , signal peptide , membrane protein , membrane , peptide sequence , helix (gastropod) , sequence (biology) , microbiology and biotechnology , gene , chemistry , organic chemistry , copolymer , polymer , ecology , snail
Summary Internal deletions close to the C‐terminus of the Escherichia coli penicillin binding protein 5 (PBP5, DacA) have defined the C‐terminal 18 residues of the protein as essential for membrane binding. This C‐terminal sequence is capable of forming a strongly amphiphilic α‐helix. In this paper we show that the PBP5 amphiphilic helix is able to anchor the periplasmic TEM‐β‐lactamase to the inner membrane. In addition, we have demonstrated that mature PBP5 (lacking the N‐terminal signal sequence) possesses the ability to bind to the membrane from a soluble form of the protein, showing that translocation across the membrane is unnecessary for anchoring to be established.