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Post-translocational folding of secretory proteins in Gram-positive bacteria

Lookup NU author(s): Professor Colin Harwood, Dr Sierd Bron


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The transport of proteins from their site of synthesis in the cytoplasm to their functional location is an essential characteristic of all living cells. In Gram-positive bacteria the majority of proteins that are translocated across the cytoplasmic membrane are delivered to the membrane-cell wall interface in an essentially unfolded form. They must then be folded into their native configuration in an environment that is dominated by a high density of immobilised negative charge - in essence an ion exchange resin. It is essential to the viability of the cell that these proteins do not block the translocation machinery in the membrane, form illegitimate interactions with the cell wall or, through intermolecular interactions, form insoluble aggregates. Native Gram-positive proteins therefore have intrinsic folding characteristics that facilitate their rapid folding, and this is assisted by a variety of folding factors, including enzymes, peptides and metal ions. Despite these intrinsic and extrinsic factors, secretory proteins do misfold, particularly if the cell is subjected to certain types of stress. Consequently, Gram-positive bacteria such as Bacillus subtilis encode membrane- and cell wall-associated proteases that act as a quality control machine, clearing misfolded or otherwise aberrant proteins from the translocase and the cell wall. © 2004 Elsevier B.V. All rights reserved.

Publication metadata

Author(s): Sarvas M, Harwood CR, Bron S, Van Dijl JM

Publication type: Review

Publication status: Published

Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Year: 2004

Volume: 1694

Issue: 1-3

Pages: 311-327

ISSN (print): 0167-4889

ISSN (electronic): 0006-3002


DOI: 10.1016/j.bbamcr.2004.04.009

PubMed id: 15546674