The sequence of sites recognised by a member of the RNase E/G family can control the maximal rate of cleavage, while a 5′-monophosphorylated end appears to function cooperatively in mediating RNA binding

Biochemical and Biophysical Research Communications

Volumn 391, Issue 1, 2010, Pages 879-883

  Jourdan, Stefanie Simone ^a   Kime, Louise ^a   McDowall, Kenneth John ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Ribonucleases; RNA binding; RNA decay and processing; RNase E G family

Indexed keywords

MESSENGER RNA; RIBONUCLEASE; RIBONUCLEASE E; RIBONUCLEASE G; UNCLASSIFIED DRUG;

ARTICLE; BINDING COMPETITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PHOSPHORYLATION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; RNA BINDING; RNA DEGRADATION; SEQUENCE ANALYSIS;

BASE SEQUENCE; ENDORIBONUCLEASES; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; NUCLEOTIDES; RNA STABILITY; RNA, BACTERIAL; RNA, MESSENGER;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 72949110938     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.11.156     Document Type: Article

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