Linked Life Data

11518522

Source:http://linkedlifedata.com/resource/pubmed/id/11518522

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-8-23
pubmed:databankReference
pubmed:abstractText
HK620 is a temperate lambdoid bacteriophage that adsorbs to the O-antigen of its host, Escherichia coli H. The genome of a temperature-sensitive clear-plaque mutant consists of 38,297 nucleotides in which we recognize 60 open reading frames (orfs). Eighteen of these lie in a region of the genome that we call the virion structure domain. The other 42 orfs lie in what we call the metabolic domain. Virions of HK620 resemble those of phage P22. The virion structural orfs encode three kinds of putative proteins relative to the virion proteins of P22: (1) those that are nearly (about 90 %) identical; (2) those that are weakly (about 30 %) identical; and (3) those composed of nearly and weakly identical segments. We hypothesize that these composite proteins form bridges between the virion proteins of the other two kinds. Three of the putative virion proteins that are only weakly identical to P22 proteins are 71, 60 and 79 % identical to proteins encoded by the phage APSE-1, whose virions also resemble those of P22. Because the hosts of APSE-1 and HK620 have been separated from each other by an estimated 200 My, we propose using the amino acid differences that have accumulated in these proteins to estimate a biological clock for temperate lambdoid phages. The putative transcriptional regulatory gene circuitry of HK620 seems to resemble that of phage lambda. Integration, on the other hand, resembles that of satellite phage P4 in that the attP sequence lies between the leftward promoter and int rather than downstream of int. Comparing the metabolic domains of several lambdoid phage genomes reveals seven short conserved sequences roughly defining boundaries of functional modules. We propose that these boundary sequences are foci of genetic recombination that serve to assort the modules and make the metabolic domain highly mosaic genetically.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
311
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
657-79
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed-meshheading:11518522-Attachment Sites, Microbiological, pubmed-meshheading:11518522-Bacteriophage P22, pubmed-meshheading:11518522-Bacteriophage lambda, pubmed-meshheading:11518522-Base Sequence, pubmed-meshheading:11518522-Chromosomes, Bacterial, pubmed-meshheading:11518522-Coliphages, pubmed-meshheading:11518522-Conserved Sequence, pubmed-meshheading:11518522-DNA Replication, pubmed-meshheading:11518522-Evolution, Molecular, pubmed-meshheading:11518522-Genes, Viral, pubmed-meshheading:11518522-Genome, Viral, pubmed-meshheading:11518522-Integrases, pubmed-meshheading:11518522-Molecular Sequence Data, pubmed-meshheading:11518522-Mutation, pubmed-meshheading:11518522-Open Reading Frames, pubmed-meshheading:11518522-Phylogeny, pubmed-meshheading:11518522-Recombination, Genetic, pubmed-meshheading:11518522-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:11518522-Viral Structural Proteins
pubmed:year
2001
pubmed:articleTitle
Nucleotide sequence of coliphage HK620 and the evolution of lambdoid phages.
pubmed:affiliation
Department of Molecular and Cell Biology, Division of Life Sciences, MS74-157, Berkeley, CA 94720, USA. ajclark@email.arizona.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.