Research output per year
Research output per year
R. L. Jack, A. Dubini, T. Palmer, F. Sargent
Research output: Contribution to journal › Article › peer-review
A subset of bacterial periplasmic enzymes are transported from the cytoplasm by the twin-arginine transport apparatus. Such proteins contain distinctive N-terminal signal peptides containing a conserved SRRXFLK 'twin-arginine' amino acid motif and often bind complex cofactors before the transport event. It is important that assembly of complex cofactor-containing, and often multi-subunit, enzymes is complete before export. Studies of the unrelated [NiFe] hydrogenase, DMSO reductase and trimethylamine N-oxide reductase systems from Escherichia coli have enabled us to define a chaperone-mediated 'proofreading' mechanism involved in co-ordinating assembly and export of twin-arginine transport-dependent enzymes.
Original language | English |
---|---|
Pages (from-to) | 105-107 |
Number of pages | 3 |
Journal | Biochemical Society Transactions |
Volume | 33 |
Issue number | 1 |
Publication status | Published - 2005 |
Event | 7th International Hydrogenases Conference - Reading, United Kingdom Duration: 24 Aug 2004 → 29 Aug 2004 |
Research output: Contribution to conference › Paper
Palmer, T. (Participant)
Activity: Participating in or organising an event types › Participation in conference
Sargent, F. (Participant)
Activity: Participating in or organising an event types › Participation in conference