Open AccessThe T at protein export pathway and its role in cyanobacterial metalloprotein biosynthesis
Author(s) -
Barnett James P.,
Robinson Colin,
Scanlan David J.,
Blindauer Claudia A.
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02391.x
Subject(s) - periplasmic space , thylakoid , twin arginine translocation pathway , metalloprotein , cytoplasm , biosynthesis , cyanobacteria , biochemistry , biology , bacterial outer membrane , microbiology and biotechnology , bacteria , escherichia coli , chloroplast , gene , enzyme , genetics
The T at 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 T at 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 T at function has been obtained from studies using E scherichia 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 T at pathway in cyanobacteria and its role in metalloprotein biosynthesis.