Prediction of twin-arginine signal peptides
Top Cited Papers
Open Access
- 2 July 2005
- journal article
- research article
- Published by Springer Nature in BMC Bioinformatics
- Vol. 6 (1) , 167
- https://doi.org/10.1186/1471-2105-6-167
Abstract
Background: Proteins carrying twin-arginine (Tat) signal peptides are exported into the periplasmic compartment or extracellular environment independently of the classical Sec-dependent translocation pathway. To complement other methods for classical signal peptide prediction we here present a publicly available method, TatP, for prediction of bacterial Tat signal peptides. Results: We have retrieved sequence data for Tat substrates in order to train a computational method for discrimination of Sec and Tat signal peptides. The TatP method is able to positively classify 91% of 35 known Tat signal peptides and 84% of the annotated cleavage sites of these Tat signal peptides were correctly predicted. This method generates far less false positive predictions on various datasets than using simple pattern matching. Moreover, on the same datasets TatP generates less false positive predictions than a complementary rule based prediction method. Conclusion: The method developed here is able to discriminate Tat signal peptides from cytoplasmic proteins carrying a similar motif, as well as from Sec signal peptides, with high accuracy. The method allows filtering of input sequences based on Perl syntax regular expressions, whereas hydrophobicity discrimination of Tat- and Sec-signal peptides is carried out by an artificial neural network. A potential cleavage site of the predicted Tat signal peptide is also reported. The TatP prediction server is available as a public web server at http://www.cbs.dtu.dk/services/TatP/.Keywords
This publication has 30 references indexed in Scilit:
- Improved Prediction of Signal Peptides: SignalP 3.0Journal of Molecular Biology, 2004
- Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coliJournal of Bacteriology, 2003
- Genetic Analysis of the Twin Arginine Translocator Secretion Pathway in BacteriaPublished by Elsevier ,2002
- In vivo dissection of the Tat translocation pathway in Escherichia coliJournal of Molecular Biology, 2002
- Unusual Signal Peptide Directs Penicillin Amidase from Escherichia coli to the Tat Translocation MachineryBiochemical and Biophysical Research Communications, 2002
- The Rieske Fe/S Protein of the Cytochromeb /f Complex in ChloroplastsJournal of Biological Chemistry, 2001
- A naturally occurring bacterial Tat signal peptide lacking one of the ‘invariant’ arginine residues of the consensus targeting motifFEBS Letters, 2001
- The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting in Escherichia coliJournal of Biological Chemistry, 2000
- Topological Rules for Membrane Protein Assembly in Eukaryotic CellsJournal of Biological Chemistry, 1997
- Sequence logos: a new way to display consensus sequencesNucleic Acids Research, 1990