A regulatory domain controls the transport activity of a twin-arginine signal peptide

FEBS Letters

Volumn 587, Issue 20, 2013, Pages 3365-3370

  Bowman, Lisa ^a   Palmer, Tracy ^a   Sargent, Frank ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

NiFe hydrogenase; Escherichia coli; Mutagenesis; Protein targeting; Signal peptide; Twin arginine translocation pathway

Indexed keywords

HYDROGENASE 1 SIGNAL PEPTIDE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN SYNTHESIS REGULATION; PROTEIN TRANSPORT; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; TWIN ARGININE TRANSLOCATION PATHWAY;

[NIFE] HYDROGENASE; ESCHERICHIA COLI; MUTAGENESIS; PROTEIN TARGETING; SIGNAL PEPTIDE; TWIN-ARGININE TRANSLOCATION PATHWAY;

AMINO ACID SEQUENCE; HYDROGENASE; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; PROTEIN SORTING SIGNALS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION;

ESCHERICHIA COLI;

EID: 84884909648     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.09.005     Document Type: Article

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