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Biochem Biophys Res Commun. 2002 Feb 15;291(1):146-9.

Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery.

Author information

1
Institut für Biotecnologie II, Technische Universität Hamburg-Harburg, Denickestrasse 15, Hamburg, 21073, Germany. ignatova@tu-harburg.de

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.

PMID:
11829474
DOI:
10.1006/bbrc.2002.6420
[Indexed for MEDLINE]

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