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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1994-5-2
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pubmed:abstractText |
Nucleotide and DNA coeffector substrate binding site characterizations were performed on two HSV-1 DNA helicases fulfilling different roles in DNA replication. Single ATP-binding sites were identified for helicase-primase and UL9 protein (Km(ATP) 0.62 mM and 0.54 mM, respectively). Analysis of structural requirements for DNA-dependent NTP hydrolysis revealed comparatively stringent requirements for helicase-primase in accommodating base-modified NTP analogs whereas the UL9 protein was much more permissive in this respect; neither enzyme was dependent on the ribose 2' or 3' hydroxyls for NTP hydrolysis. Both helicase-primase and UL9 protein ATPase activities were inhibited by ADP or GDP; this effect was competitive rather than allosteric. The enhancement of ATPase activity on a single stranded (ss) DNA substrate as opposed to double stranded (ds) DNA was much more marked for helicase-primase than for the UL9 protein (Km(dsDNA)/Km(ssDNA) 60 and 9, respectively). The triphosphates of the antiviral agents acyclovir and penciclovir were not effective substrates for either helicase-primase or UL9 protein.
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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/Acid Anhydride Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Superhelical,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Triphosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/UL9 protein, Human herpesvirus 1,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
199
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1333-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8147877-Acid Anhydride Hydrolases,
pubmed-meshheading:8147877-Adenosine Triphosphatases,
pubmed-meshheading:8147877-Binding Sites,
pubmed-meshheading:8147877-DNA,
pubmed-meshheading:8147877-DNA, Single-Stranded,
pubmed-meshheading:8147877-DNA, Superhelical,
pubmed-meshheading:8147877-DNA Helicases,
pubmed-meshheading:8147877-DNA Primase,
pubmed-meshheading:8147877-DNA Replication,
pubmed-meshheading:8147877-DNA-Binding Proteins,
pubmed-meshheading:8147877-Deoxyribonucleotides,
pubmed-meshheading:8147877-Herpesvirus 1, Human,
pubmed-meshheading:8147877-Kinetics,
pubmed-meshheading:8147877-Nucleoside-Triphosphatase,
pubmed-meshheading:8147877-RNA Nucleotidyltransferases,
pubmed-meshheading:8147877-Recombinant Proteins,
pubmed-meshheading:8147877-Ribonucleotides,
pubmed-meshheading:8147877-Substrate Specificity,
pubmed-meshheading:8147877-Viral Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Characterisation of the nucleotide and DNA coeffector binding sites of the herpes simplex virus type 1 (HSV-1) encoded helicase-primase complex and UL9 origin binding protein.
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pubmed:affiliation |
SmithKline Beecham Pharmaceuticals, Harlow, Essex, U.K.
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pubmed:publicationType |
Journal Article
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