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Unusual Signal Peptide Directs Penicillin Amidase From Escherichia Coli to the Tat Translocation Machinery

Unusual Signal Peptide Directs Penicillin Amidase From Escherichia Coli to the Tat Translocation Machinery

Zoya Ignatova, Claudia Hörnle, Alan Nurk, Volker Kasche

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

PMID: 11829474

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9014066	Penicillin Amidase from Escherichia coli		9014-06-6	Price

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