Barnett, James P., Robinson, Colin, Scanlan, David J. and Blindauer, Claudia A. (2011) The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis. FEMS Microbiology Letters, Vol.325 (No.1). pp. 1-9. doi:10.1111/j.1574-6968.2011.02391.x

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Abstract

The Tat pathway is a common protein translocation system that is found in the bacterial cytoplasmic membrane, as well as in the cyanobacterial and plant thylakoid membranes. It is unusual in that the Tat pathway transports fully folded, often metal cofactor-containing proteins across these membranes. In bacteria, the Tat pathway plays an important role in the biosynthesis of noncytoplasmic metalloproteins. By compartmentalizing protein folding to the cytoplasm, the potentially aberrant binding of non-native metal ions to periplasmic proteins is avoided. To date, most of our understanding of Tat function has been obtained from studies using Escherichia coli as a model organism but cyanobacteria have an extra layer of complexity with proteins targeted to both the cytoplasmic and thylakoid membranes. We examine our current understanding of the Tat pathway in cyanobacteria and its role in metalloprotein biosynthesis.

Item Type:	Journal Article
Subjects:	Q Science > Q Science (General)
Divisions:	Faculty of Science > Chemistry Faculty of Science > Life Sciences (2010- )
Journal or Publication Title:	FEMS Microbiology Letters
Publisher:	Wiley-Blackwell Publishing Ltd.
ISSN:	0378-1097
Official Date:	2011
Dates:	Date Event 2011 Published
Volume:	Vol.325
Number:	No.1
Number of Pages:	9
Page Range:	pp. 1-9
DOI:	10.1111/j.1574-6968.2011.02391.x
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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