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  Import of periplasmic bacteriocins targeting the murein

Braun, V., Helbig, S., & Patzer, S. (2012). Import of periplasmic bacteriocins targeting the murein. Biochemical Society Transactions, 40(6), 1449-1455. doi:10.1042/BST20120175.

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 Creators:
Braun, V1, Author           
Helbig, S1, Author           
Patzer, SI1, Author           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              

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 Abstract: Colicins are the only proteins imported by Escherichia coli and thus serve as tools to study the protein import mechanism. Most of the colicins studied degrade DNA, 16S RNA or tRNA in the cytoplasm, or form pores in the cytoplasmic membrane. Two bacteriocins, Cma (colicin M) and Pst (pesticin), affect the murein structure in the periplasm. These two bacteriocins must be imported only across the outer membrane and therefore represent the simplest system for studying protein import. Cma can be reversibly translocated across the outer membrane. Cma and Pst unfold during import. The crystal structure of Pst reveals a phage T4L (T4 lysozyme) fold of the activity domain. Both bacteriocins require energy for import which is translocated from the cytoplasmic membrane into the outer membrane by the Ton system. Cma kills cells only when the periplasmic FkpA PPIase (peptidylprolyl cis-trans isomerase)/chaperone is present.

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 Dates: 2012-12
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1042/BST20120175
PMID: 23176497
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Title: Biochemical Society Transactions
  Other : Biochem Soc Trans
Source Genre: Journal
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Publ. Info: London, UK : Portland Press
Pages: - Volume / Issue: 40 (6) Sequence Number: - Start / End Page: 1449 - 1455 Identifier: ISSN: 0300-5127
CoNE: https://pure.mpg.de/cone/journals/resource/954925507337