Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites

Nucleic Acids Research

Volumn 35, Issue 9, 2007, Pages 3016-3031

  Allemand, F ^a   Haentjens, J ^a   Chiaruttini, C ^a   Royer, C ^b,c   Springer, Mathias ^a  

^a CNRS   (France)

^b INSERM   (France)

^c CENTRE DE BIOCHIMIE STRUCTURALE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEIN L20; RIBOSOME PROTEIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; RPLT PROTEIN, E COLI;

ARTICLE; BACTERIAL GENETICS; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; DIMERIZATION; ESCHERICHIA COLI; FLUORESCENCE CORRELATION SPECTROSCOPY; GEL FILTRATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN RNA BINDING; RNA PROBE; AFFINITY CHROMATOGRAPHY; CHEMISTRY; CONFORMATION; GEL CHROMATOGRAPHY; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OPERATOR GENE; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; SPECTROFLUOROMETRY;

ESCHERICHIA COLI;

BASE SEQUENCE; BINDING SITES; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, GEL; ESCHERICHIA COLI PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; OPERATOR REGIONS (GENETICS); PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; RIBOSOMAL PROTEINS; RNA, MESSENGER; SPECTROMETRY, FLUORESCENCE;

EID: 34250634486     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm197     Document Type: Article

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