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Volumn 177, Issue 1, 2001, Pages 107-112

A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif

Author keywords

Escherichia coli; Suppression mutagenesis; Tat protein export pathway; TMAO reductase; Twin arginine signal peptide

Indexed keywords

ARGININE; ASPARTIC ACID; BENZYLVIOLOGEN; GLYCEROL; LYSINE; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN; TRIMETHYLAMINE OXIDE;

EID: 0036136514     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-001-0366-2     Document Type: Article
Times cited : (47)

References (38)
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    • The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
    • (1999) Eur J Biochem , vol.263 , pp. 543-551
    • Halbig, D.1    Wiegert, T.2    Blaudeck, N.3    Freudl, R.4    Sprenger, G.A.5
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    • Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation
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    • Sambasivarao, D.1    Weiner, J.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.