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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-4-30
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pubmed:abstractText |
cosB is the binding site on lambda DNA for terminase, the phage DNA packaging protein. cosB contains three binding sites for gpNu1, the small subunit of terminase, and a site for integration host factor (IHF). IHF plays an accessory role in lambda DNA packaging, and IHF stimulates the burst size of lambda several-fold, presumably by assisting the interaction of terminase with cosB. The present work includes a study of the effect on lambda development of a mutation, called I1A-, which consists of three adjacent base-pair changes in the IHF binding site. The I1A- mutation was found to abolish IHF stimulation of the lambda burst size, indicating that IHF is unable to bind to the mutant I1A site. A second mutation, called I1B- and also consisting of three adjacent base-pair changes, is a mutation that reduces an intrinsic bend found in cosB. lambda I1B- was more dependent on IHF than lambda+, raising the possibility that the intrinsic bend in cosB plays a role in cos function for lambda+ under the IHF- conditions. In vitro DNA packaging experiments established that the I1 mutations affect DNA packaging per se. A series of Nu1 mutations that create terminases able to suppress a variety of cosB defects were found to suppress the defects of the I1A- and I1B- mutations under IHF- conditions.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Integration Host Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/terminase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
230
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
505-15
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8464062-Bacterial Proteins,
pubmed-meshheading:8464062-Bacteriophage lambda,
pubmed-meshheading:8464062-Base Sequence,
pubmed-meshheading:8464062-Binding Sites,
pubmed-meshheading:8464062-DNA, Viral,
pubmed-meshheading:8464062-DNA-Binding Proteins,
pubmed-meshheading:8464062-Endodeoxyribonucleases,
pubmed-meshheading:8464062-Escherichia coli,
pubmed-meshheading:8464062-Integration Host Factors,
pubmed-meshheading:8464062-Molecular Sequence Data,
pubmed-meshheading:8464062-Mutagenesis, Site-Directed,
pubmed-meshheading:8464062-Nucleic Acid Conformation,
pubmed-meshheading:8464062-Oligodeoxyribonucleotides,
pubmed-meshheading:8464062-Phenotype,
pubmed-meshheading:8464062-Plasmids,
pubmed-meshheading:8464062-Suppression, Genetic
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pubmed:year |
1993
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pubmed:articleTitle |
Function of IHF in lambda DNA packaging. II. Effects of mutations altering the IHF binding site and the intrinsic bend in cosB on lambda development.
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pubmed:affiliation |
Genetics Ph.D. Program, University of Iowa, Iowa City 52242.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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