A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif

FEBS Letters

Volumn 497, Issue 1, 2001, Pages 45-49

  Hinsley, Andrew P ^a   Stanley, Nicola R ^a,b   Palmer, Tracy ^a,b   Berks, Ben C ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b JOHN INNES CENTRE   (United Kingdom)

Author keywords

Bacterial protein export; Rieske protein; Sec independent; Tat pathway; Tetrathionate reductase; Twin arginine signal peptide

Indexed keywords

ARGININE; BACTERIAL PROTEIN; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL ORGANELLE; CONTROLLED STUDY; ELECTRON TRANSPORT; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN TRANSPORT; SALMONELLA ENTERICA;

AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; ARGININE; BACTERIAL PROTEINS; CONSENSUS SEQUENCE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; SALMONELLA ENTERICA; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBCELLULAR FRACTIONS;

BACTERIA (MICROORGANISMS); SALMONELLA ENTERICA;

EID: 0035907063     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(01)02428-0     Document Type: Article

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