Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/54874
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Type: Journal article
Title: Characterisation of Tat protein transport complexes carrying inactivating mutations
Author: McDevitt, C.
Hicks, M.
Palmer, T.
Berks, B.
Citation: Biochemical and Biophysical Research Communications, 2005; 329(2):693-698
Publisher: Academic Press Inc
Issue Date: 2005
ISSN: 0006-291X
1090-2104
Statement of
Responsibility: 
Christopher A. McDevitt, Matthew G. Hicks, Tracy Palmer, Ben C. Berks
Abstract: The Tat system functions to transport folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. Tat transport involves a high molecular weight TatBC-containing complex that transiently associates with TatA during protein translocation. Sedimentation equilibrium experiments were used to determine a protein-only molecular mass for the TatBC complex of 630+/-30kDa, suggesting that it contains approximately 13 copies of the TatB and TatC protomers. Point mutations that inactivate Tat transport have previously been identified in each of TatA, TatB, and TatC. Analysis of the TatBC complexes formed by these inactive variants demonstrates that the amino acid substitutions neither affect the composition of the TatBC complex nor cause accumulation of the assembled TatABC translocation site. In addition, the TatA protein is shown not to be required for the assembly or stability of the TatBC complex.
Keywords: Escherichia coli; Tat protein transport; Twin-arginine translocation
RMID: 0020093545
DOI: 10.1016/j.bbrc.2005.02.038
Appears in Collections:Molecular and Biomedical Science publications

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