PMID:11829474

Citation	Ignatova, Z, Hörnle, C, Nurk, A and Kasche, V (2002) Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery. Biochem. Biophys. Res. Commun. 291:146-9
Abstract	The recently described Tat protein translocation system in Escherichia coli recognizes its protein substrates by the consensus twin arginine (SRRXFLK) motif in the signal peptide. The signal sequence of E. coli pre-pro-penicillin amidase bears two arginine residues separated by one aspargine and does not resemble the Tat-targeting motif but can nevertheless target the precursor to the Tat pathway. Mutational studies have shown that the hydrophobic core region acts in synergism with the positive charged N-terminal part of the signal peptide as a Tat recognition signal and contributes to the efficient Tat targeting of the pre-pro-penicillin amidase.
Links	PubMed Online version:10.1006/bbrc.2002.6420
Keywords	Amino Acid Motifs/physiology; Amino Acid Sequence; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Transport Proteins/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed; Penicillin Amidase/genetics; Penicillin Amidase/metabolism; Protein Processing, Post-Translational/physiology; Protein Sorting Signals/physiology; Protein Transport/physiology; Structure-Activity Relationship
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.