A common export pathway for proteins binding complex redox cofactors?

BC Berks - Molecular microbiology, 1996 - Wiley Online Library
The precursor polypeptides of periplasmic proteins binding seven types of redox cofactor
have unusually long signal sequences bearing a consensus (S/T)‐R‐R‐x‐F‐L‐K motif …

The Tat protein export pathway

BC Berks, F Sargent, T Palmer - Molecular microbiology, 2000 - Wiley Online Library
The Tat (twin‐arginine translocation) system is a bacterial protein export pathway with the
remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins …

[HTML][HTML] Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions

BC Berks, SJ Ferguson, JWB Moir… - Biochimica et Biophysica …, 1995 - Elsevier
Nitrogen is present in the environment in a number of oxidation states (Fig. 1). Interconversion
between these oxidation states is predominantly biological (Fig. 1). In this review we …

[HTML][HTML] Overlapping functions of components of a bacterial Sec‐independent protein export pathway

…, NR Stanley, M Wexler, C Robinson, BC Berks… - The EMBO …, 1998 - embopress.org
We describe the identification of two Escherichia coli genes required for the export of
cofactor‐containing periplasmic proteins, synthesized with signal peptides containing a twin …

The twin-arginine translocation (Tat) protein export pathway

T Palmer, BC Berks - Nature Reviews Microbiology, 2012 - nature.com
… Examples are single-polypeptide c-type haem- and flavin-binding flavocytochromes c 33
and the c-type haem- and Cu Z copper–sulphur cluster-containing nitrous oxide reductase of …

[HTML][HTML] An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria

…, F Sargent, NR Stanley, BC Berks, C Robinson… - Journal of Biological …, 1998 - ASBMB
Proteins are transported across the bacterial plasma membrane and the chloroplast thylakoid
membrane by means of protein translocases that recognize N-terminal targeting signals in …

The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter

…, T Palmer, HR Saibil, BC Berks - Proceedings of the …, 2005 - National Acad Sciences
The Tat system mediates Sec-independent transport of folded precursor proteins across the
bacterial plasma membrane or the chloroplast thylakoid membrane. Tat transport involves …

[HTML][HTML] Sec-independent protein translocation in Escherichia coli: a distinct and pivotal role for the TatB protein

F Sargent, NR Stanley, BC Berks, T Palmer - Journal of Biological …, 1999 - ASBMB
In Escherichia coli, transmembrane translocation of proteins can proceed by a number of
routes. A subset of periplasmic proteins are exported via the Tat pathway to which proteins are …

[HTML][HTML] The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli

NR Stanley, T Palmer, BC Berks - Journal of Biological Chemistry, 2000 - ASBMB
In Escherichia coli a subset of periplasmic proteins is exported through the Tat pathway to
which substrates are directed by an NH 2 -terminal signal peptide containing a consensus …

A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system

SC Andrews, BC Berks, J McClay, A Ambler… - …, 1997 - microbiologyresearch.org
The nucleotide sequence has been determined for a twelve-gene operon of Escherichia
coli designated the hyf operon (hyfABCDEFGHIR-focB). The hyf operon is located at 55.8-56.0 …