Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome

Journal of Biological Chemistry

Volumn 282, Issue 3, 2007, Pages 2019-2028

  Odaert, Benoît ^a,b,e   Saïda, Fakhri ^a,f   Aliprandi, Pascale ^a,b   Durand, Sylvain ^c   Créchet, Jean Bernard ^a,b   Guerois, Raphaël ^d   Laalami, Soumaya ^c   Uzan, Marc ^c   Bontems, François ^a,b  

^a INSTITUT DE CHIMIE DES SUBSTANCES NATURELLES   (France)

^b ECOLE POLYTECHNIQUE   (France)

^c INSTITUT JACQUES MONOD   (France)

^d CEA SACLAY   (France)

^e INSTITUT EUROPÉEN DE CHIMIE ET BIOLOGIE   (France)

^f UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGES; CATALYSIS; ESCHERICHIA COLI; PROTEINS;

MUTANTS; RIBOSOMES; TRANSLATION INITIATION SITES;

ENZYME KINETICS;

MESSENGER RNA; MUTANT PROTEIN; REGB ENDORIBONUCLEASE; RIBONUCLEASE; RIBONUCLEASE REL E; RIBONUCLEASE YOE B; RNA; UNCLASSIFIED DRUG; BACTERIAL TOXIN; ESCHERICHIA COLI PROTEIN; RELE PROTEIN, E COLI; YOEB PROTEIN, E COLI;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; INHIBITION KINETICS; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; RIBOSOME; RNA ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; TRANSLATION INITIATION; TRANSLATION REGULATION; BACTERIOPHAGE T4; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN SYNTHESIS; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

AMINO ACID SEQUENCE; BACTERIAL TOXINS; BACTERIOPHAGE T4; CATALYTIC DOMAIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; RIBONUCLEASES; RIBOSOMES; RNA, MESSENGER;

EID: 33847304137     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M608271200     Document Type: Article

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