Activation of the RegB endoribonuclease by the S1 ribosomal protein is due to cooperation between the S1 four C-terminal modules in a substrate-dependant manner

Journal of Biological Chemistry

Volumn 278, Issue 17, 2003, Pages 15261-15271

  Bisaglia, Marco ^a   Laalami, Soumaya ^b   Uzan, Marc ^b   Bontems, François ^a  

^a ECOLE POLYTECHNIQUE   (France)

^b INSTITUT JACQUES MONOD   (France)

Author keywords

[No Author keywords available]

Indexed keywords

GENES; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEINS; RNA; SUBSTRATES;

NUCLEOTIDES;

BIOCHEMISTRY;

AMINO ACID DERIVATIVE; MESSENGER RNA; NUCLEOTIDE DERIVATIVE; PROTEIN REGB; RIBONUCLEASE; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIOPHAGE T4; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVATION; ENZYME DEGRADATION; ENZYME SUBSTRATE COMPLEX; GENETIC CONSERVATION; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; RNA METABOLISM;

AMINO ACID SEQUENCE; ENDORIBONUCLEASES; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RIBOSOMAL PROTEINS;

T4 BACTERIOPHAGE;

EID: 0037674539     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M212731200     Document Type: Article

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