The Antitermin ation Activity of Bacteriophage λ N Protein is Controlled by the Kinetics of an RNA-Looping-Facilitated Interaction with the Transcription Complex

Journal of Molecular Biology

Volumn 384, Issue 1, 2008, Pages 87-108

  Conant, Clarke R ^a   Goodarzi, Jim P ^a   Weitzel, Steven E ^a   von Hippel, Peter H ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

antitermination; enhancers; looping; nonspecific binding; transcription

Indexed keywords

BACTERIAL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN BOXB; RNA POLYMERASE; UNCLASSIFIED DRUG; DNA DIRECTED RNA POLYMERASE; ELONGATION FACTOR; MESSENGER RNA; N PROTEIN, BACTERIOPHAGE LAMBDA; VIRUS DNA; VIRUS PROTEIN; VIRUS RNA;

ARTICLE; BACTERIOPHAGE LAMBDA; COMPLEX FORMATION; CONTROLLED STUDY; GENE ACTIVITY; IN VITRO STUDY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN INTERACTION; REGULATOR GENE; RNA TRANSCRIPTION; RNA TRANSLATION; BINDING SITE; BIOLOGICAL MODEL; CHEMISTRY; CONFORMATION; DNA TEMPLATE; GENETIC TRANSCRIPTION; GENETICS; METABOLISM; STOP CODON;

ENTEROBACTERIA PHAGE LAMBDA; ESCHERICHIA COLI;

BACTERIOPHAGE LAMBDA; BINDING SITES; CODON, TERMINATOR; DNA, VIRAL; DNA-DIRECTED RNA POLYMERASES; KINETICS; MODELS, GENETIC; NUCLEIC ACID CONFORMATION; PEPTIDE ELONGATION FACTORS; PROTEIN BINDING; RNA, MESSENGER; RNA, VIRAL; TEMPLATES, GENETIC; TRANSCRIPTION, GENETIC; VIRAL REGULATORY AND ACCESSORY PROTEINS;

EID: 54249128774     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.014     Document Type: Article

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