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rdf:type |
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lifeskim:mentions |
umls-concept:C0067096,
umls-concept:C0085862,
umls-concept:C0185026,
umls-concept:C0205147,
umls-concept:C0599945,
umls-concept:C1299583,
umls-concept:C1514562,
umls-concept:C1549571,
umls-concept:C1608386,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
2
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pubmed:dateCreated |
1998-7-27
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pubmed:abstractText |
The transcriptional antitermination protein N of bacteriophage lambda binds the boxB component of the RNA enhancer nut (boxA + boxB) and the E. coli elongation factor NusA. Efficient antitermination by N requires an RNA-binding domain (amino acids 1-22) and two activating regions for antitermination: a newly identified NusA-binding region (amino acids 34-47) that suppresses NusA's enhancement of termination, and a carboxy-terminal region (amino acids 73-107) that interacts directly with RNA polymerase. Heteronuclear magnetic resonance experiments demonstrate that N is a disordered protein. Interaction with boxB RNA induces only the RNA-binding domain of N to adopt a folded conformation, while the activating regions of the protein remain disordered in the absence of their target proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/N protein, Bacteriophage lambda,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Regulatory and Accessory...,
http://linkedlifedata.com/resource/pubmed/chemical/nusA protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-75
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9659923-Amino Acid Sequence,
pubmed-meshheading:9659923-Bacterial Proteins,
pubmed-meshheading:9659923-Bacteriophage lambda,
pubmed-meshheading:9659923-Binding Sites,
pubmed-meshheading:9659923-DNA-Directed RNA Polymerases,
pubmed-meshheading:9659923-Enhancer Elements, Genetic,
pubmed-meshheading:9659923-Escherichia coli Proteins,
pubmed-meshheading:9659923-Gene Expression Regulation, Viral,
pubmed-meshheading:9659923-Ligands,
pubmed-meshheading:9659923-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9659923-Molecular Sequence Data,
pubmed-meshheading:9659923-Peptide Elongation Factors,
pubmed-meshheading:9659923-Peptide Fragments,
pubmed-meshheading:9659923-Protein Structure, Tertiary,
pubmed-meshheading:9659923-RNA, Viral,
pubmed-meshheading:9659923-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:9659923-Transcription Factors,
pubmed-meshheading:9659923-Viral Regulatory and Accessory Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein.
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pubmed:affiliation |
Banting and Best Department of Medical Research, Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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