reviewTop 1% cited
The Tat protein export pathway
Molecular Microbiology · 2000 · Vol. 35(2) · pp. 260–274
Ben C. Berks✉(University of East Anglia)Frank Sargent(University of East Anglia)Tracy Palmer(University of East Anglia)
Abstract
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 are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway.
Trace Elements in HealthEnzyme Structure and FunctionRNA and protein synthesis mechanismsBiologyTwin-arginine translocation pathwayCytoplasmArginineTransport proteinCell biologyChromosomal translocationSignal peptideTransloconBiochemistry
MeSH terms
Amino Acid SequenceBacterial ProteinsBiological TransportCell MembraneGram-Negative BacteriaMolecular Sequence DataProtein FoldingProtein Sorting Signals
Citations
577
FWCI
43.51
field-weighted impact
References
123
Percentile
100%
vs. same field & year
Citations per year
Cited by
Improved Prediction of Signal Peptides: SignalP 3.0
Journal of Molecular Biology · 2004 · 6,350 citations
References
Signal sequences
Journal of Molecular Biology · 1985 · 2,178 citations
<b>A common export pathway for proteins binding complex redox cofactors?</b>
Molecular Microbiology · 1996 · 661 citations
Membrane protein structure prediction
Journal of Molecular Biology · 1992 · 1,673 citations
Citation Network
How this paper connects to the literature. Drag to explore, click any node to open that paper.
