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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1989-4-3
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pubmed:abstractText |
By means of comparative analysis of primary and secondary structures, and hydropathy plots of hepadnavirus P proteins new functional domains were revealed additionally to the polymerase domain which had been found earlier in these proteins. The C-terminal part of P proteins was revealed to be significantly similar to ribonuclease H of E. coli. The ribonuclease H functional domain is known to be an integral entity of retrovirus reverse transcriptase as a rule. Availability of this domain indicates once more the putative reverse transcriptase properties of the P products. The proteins of hepadnaviruses were compared to terminal proteins of picornaviruses, adenoviruses and bacteriophages. The data obtained suggested that a conservative N-terminal region of P proteins functions as protein primer for DNA synthesis in hepadnaviruses.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease H,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
243
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2465182-Amino Acid Sequence,
pubmed-meshheading:2465182-DNA-Directed DNA Polymerase,
pubmed-meshheading:2465182-Endoribonucleases,
pubmed-meshheading:2465182-Escherichia coli,
pubmed-meshheading:2465182-Genes, Viral,
pubmed-meshheading:2465182-Hepatitis Viruses,
pubmed-meshheading:2465182-Molecular Sequence Data,
pubmed-meshheading:2465182-Protein Conformation,
pubmed-meshheading:2465182-RNA-Directed DNA Polymerase,
pubmed-meshheading:2465182-Ribonuclease H,
pubmed-meshheading:2465182-Viral Proteins
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pubmed:year |
1989
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pubmed:articleTitle |
Prediction of terminal protein and ribonuclease H domains in the gene P product of hepadnaviruses.
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pubmed:affiliation |
D.I. Ivanovsky Institute of Virology, Academy of Medical Sciences, Moscow, USSR.
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pubmed:publicationType |
Journal Article,
Comparative Study
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