Impact of amino acid changes in the signal peptide on the secretion of the Tat-dependent xylanase C from Streptomyces lividans.

doi:10.1111/j.1574-6968.2005.00081.x

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Article

Impact of amino acid changes in the signal peptide on the secretion of the Tat-dependent xylanase C from Streptomyces lividans.

FEMS microbiology letters - 1 Feb 2006

Li Haiming, Faury Damien, Morosoli Rolf

Abstract excerpt

Xylanase C (XlnC) is a cofactorless protein secreted through the twin arginine translocation (Tat)-dependent secretion pathway by Streptomyces lividans. Its signal peptide contains the SRRGFLG sequence, which is similar to the twin-arginine consensus motif. The 49 amino acid-long signal peptide was analyzed by random, site-directed and site-saturation mutagenesis and the effect of these mutations on XlnC...

Topics

Amino Acid Sequence
Endo-1,4-beta Xylanases
Escherichia coli Proteins
Membrane Transport Proteins
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Protein Sorting Signals
Streptomyces lividans

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Identifiers

PMID: 16448505
DOI: 10.1111/j.1574-6968.2005.00081.x

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