| pubmed-article:7816603 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7816603 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:7816603 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:7816603 | lifeskim:mentions | umls-concept:C0012892 | lld:lifeskim |
| pubmed-article:7816603 | lifeskim:mentions | umls-concept:C0445223 | lld:lifeskim |
| pubmed-article:7816603 | lifeskim:mentions | umls-concept:C1552599 | lld:lifeskim |
| pubmed-article:7816603 | lifeskim:mentions | umls-concept:C1704787 | lld:lifeskim |
| pubmed-article:7816603 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:7816603 | pubmed:dateCreated | 1995-2-3 | lld:pubmed |
| pubmed-article:7816603 | pubmed:abstractText | In order to establish the evolutionary relationship between the family A and B DNA polymerases, we have closely compared the 3'-->5' exonuclease domains between the Klenow fragment of E.coli DNA polymerase I (a family A DNA polymerase) and the bacteriophage PRD1 DNA polymerase, the smallest member of the DNA polymerase family B. Although the PRD1 DNA polymerase has a smaller 3'-->5' exonuclease domain, its active sites appear to be very similar to those of the Klenow fragment. Site-directed mutagenesis studies revealed that the residues important for the 3'-->5' exonuclease activity, particularly metal binding ligands for the Klenow fragment, are all conserved in the PRD1 DNA polymerase as well. The metal binding ligands are also essential for the strand-displacement activity of the PRD1 DNA polymerase. Based on these results and the studies by others in various systems, we conclude that family A and B DNA polymerases, at least in the 3'-->5' exonuclease domain, are structurally as well as evolutionarily related. | lld:pubmed |
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| pubmed-article:7816603 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7816603 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7816603 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7816603 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7816603 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7816603 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:7816603 | pubmed:author | pubmed-author:ItoJJ | lld:pubmed |
| pubmed-article:7816603 | pubmed:author | pubmed-author:ZhuWW | lld:pubmed |
| pubmed-article:7816603 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7816603 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:7816603 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:7816603 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7816603 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7816603 | pubmed:pagination | 5177-83 | lld:pubmed |
| pubmed-article:7816603 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:7816603 | pubmed:meshHeading | pubmed-meshheading:7816603-... | lld:pubmed |
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| pubmed-article:7816603 | pubmed:meshHeading | pubmed-meshheading:7816603-... | lld:pubmed |
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| pubmed-article:7816603 | pubmed:meshHeading | pubmed-meshheading:7816603-... | lld:pubmed |
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| pubmed-article:7816603 | pubmed:meshHeading | pubmed-meshheading:7816603-... | lld:pubmed |
| pubmed-article:7816603 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7816603 | pubmed:articleTitle | Family A and family B DNA polymerases are structurally related: evolutionary implications. | lld:pubmed |
| pubmed-article:7816603 | pubmed:affiliation | Department of Microbiology and Immunology, College of Medicine, University of Arizona, Tucson 85724. | lld:pubmed |
