TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli
Matos, Cristina F. R. O., Di Cola, Alessandra and Robinson, Colin. (2009) TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli. EMBO reports, Vol.10 (No.5). pp. 474-479. ISSN 1469-221XFull text not available from this repository.
Official URL: http://dx.doi.org/10.1038/embor.2009.34
Bacterial Tat systems export folded proteins, including FeS proteins such as NrfC and NapG, which acquire their cofactors before translocation. NrfC and NapG are proofread by the Tat pathway, and misfolded examples are degraded after interaction with the translocon. Here, we identify TatD as a crucial component of this quality control system in Escherichia coli. NrfC/NapG variants lacking FeS centres are rapidly degraded in wild-type cells but stable in a DtatD strain. The precursor of another substrate, FhuD, is also transiently detected in wild-type cells but stable in the DtatD strain. Surprisingly, these substrates are stable in DtatD cells that overexpress TatD, and export of the non-mutated precursors is inhibited. We propose that TatD is part of a quality control system that is intimately linked to the Tat export pathway, and that the overexpression of TatD leads to an imbalance between the two systems such that both Tat-initiated turnover and export are prevented.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Divisions:||Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)|
|Journal or Publication Title:||EMBO reports|
|Publisher:||Nature Publishing Group|
|Number of Pages:||6|
|Page Range:||pp. 474-479|
|Access rights to Published version:||Restricted or Subscription Access|
|Funder:||Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), European Union (EU)|
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