Translational operator of mRNA on the ribosome: How repressor proteins exclude ribosome binding

Science

Volumn 308, Issue 5718, 2005, Pages 120-123

  Jenner, Lasse ^a   Romby, Pascale ^b   Rees, Bernard ^a   Schulze Briese, Clemens ^c   Springer, Mathias ^d   Ehresmann, Chantal ^b   Ehresmann, Bernard ^b   Moras, Dino ^a   Yusupova, Gulnara ^a   Yusupov, Marat ^a,b  

^a INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^b INSTITUT DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

^d INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELLS; CRYSTAL STRUCTURE; CRYSTALLIZATION; CYTOLOGY;

RIBOSOMES; THERMUS THERMOPHILUS; TRANSFER RNA (TRNA); TRANSLATIONAL OPERATOR;

RNA;

MESSENGER RNA; REPRESSOR PROTEIN; BACTERIAL PROTEIN; BACTERIAL RNA; METHIONINE TRANSFER RNA; RIBOSOME PROTEIN; RNA 16S; THREONINE TRANSFER RNA LIGASE;

RNA;

ARTICLE; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; CRYSTALLIZATION; GENE EXPRESSION REGULATION; MESSENGER RNA SYNTHESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; RIBOSOME; RIBOSOME SUBUNIT; RNA TRANSLATION; TASK PERFORMANCE; TRANSLATION INITIATION; X RAY CRYSTALLOGRAPHY; BASE PAIRING; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; FOURIER ANALYSIS; GENETICS; METABOLISM; PROTEIN SYNTHESIS; REGULATORY RNA SEQUENCE; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

BACTERIAL PROTEINS; BASE PAIRING; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; FOURIER ANALYSIS; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN BIOSYNTHESIS; REGULATORY SEQUENCES, RIBONUCLEIC ACID; REPRESSOR PROTEINS; RIBOSOMAL PROTEINS; RIBOSOMES; RNA, BACTERIAL; RNA, MESSENGER; RNA, RIBOSOMAL, 16S; RNA, TRANSFER, MET; THERMUS THERMOPHILUS; THREONINE-TRNA LIGASE;

EID: 20144388921     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1105639     Document Type: Article

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27. This work was funded by CNRS (French National Center for Scientific Research). We thank H. Noller, J. Cate, and J. Doudna for critical reading of the manuscript; C. Branlant for support of this work; B. Klaholz, S. Marzi, M. Rodnina, and D. Wilson for helpful discussions; G. Keith for analysis of tRNA in ribosome samples; F. Winter for help in the mRNA preparation; D. Rose for growing T. thermophilus cells; M. Ruff and J.-C. Thierry for preliminary synchrotron experiments; and T. Petrova for her help in an initial stage of molecular replacement calculations. Coordinates and structure factors have been deposited in the Protein Data Bank with accession codes 1YL3 and 1YL4.