Linked Life Data

2850009

Source:http://linkedlifedata.com/resource/pubmed/id/2850009

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1989-2-13
pubmed:abstractText
The structural and functional organization of the herpes simplex virus type I (HSV-1) DNA polymerase enzyme of strain ANG was studied by a combination of sequence and immunobiochemical analyses. Comparison of the HSV-1 ANG DNA polymerase sequence with those of pro- and eukaryotic DNA polymerases resulted in the allocation of eleven conserved regions within the HSV-1 DNA polymerase. From the analysis of all currently identified mutations of temperature-sensitive and drug-resistant HSV-1 DNA polymerase mutants as well as from the degree of conservancy observed, it could be deduced that the amino-acid residues 597-961, comprising the homologous sequence regions IV-IX, constitute the major structural components of the catalytic domain of the enzyme which should accommodate the sites for polymerizing and 3'-to-5' exonucleolytic functions. Further insight into the structural organization was gained by the use of polyclonal antibodies responding specifically to the N-terminal, central and C-terminal polypeptide domains of the ANG polymerase. Each of the antisera was able to immunostain as well as to immunoprecipitate a viral polypeptide of 132 +/- 5 kDa that corresponded well to the molecular mass of 136 kDa predicted from the coding sequences. Enzyme-binding and neutralization studies confirmed that both functions, polymerase and 3'-to-5' exonuclease, are intimately related to each other, and revealed that, in addition to the sequences of the proposed catalytic domain, the very C-terminal sequences, except for amino-acid residues 1072-1146, are important for the catalytic functions of the enzyme, most likely effecting the binding to DNA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
951
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
298-314
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2850009-Amino Acid Sequence, pubmed-meshheading:2850009-Base Sequence, pubmed-meshheading:2850009-Binding Sites, pubmed-meshheading:2850009-Catalysis, pubmed-meshheading:2850009-DNA Restriction Enzymes, pubmed-meshheading:2850009-DNA-Directed DNA Polymerase, pubmed-meshheading:2850009-Exodeoxyribonuclease V, pubmed-meshheading:2850009-Exodeoxyribonucleases, pubmed-meshheading:2850009-Immune Sera, pubmed-meshheading:2850009-Immunosorbent Techniques, pubmed-meshheading:2850009-Molecular Sequence Data, pubmed-meshheading:2850009-Molecular Weight, pubmed-meshheading:2850009-Mutation, pubmed-meshheading:2850009-Peptide Fragments, pubmed-meshheading:2850009-Sequence Homology, Nucleic Acid, pubmed-meshheading:2850009-Simplexvirus, pubmed-meshheading:2850009-Structure-Activity Relationship
pubmed:year
1988
pubmed:articleTitle
The herpes simplex virus DNA polymerase: analysis of the functional domains.
pubmed:affiliation
Institut für Virusforschung, Deutsches Krebsforschungszentrum, Heidelberg, F.R.G.
pubmed:publicationType
Journal Article, Comparative Study