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rdf:type |
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lifeskim:mentions |
umls-concept:C0002520,
umls-concept:C0005456,
umls-concept:C0012854,
umls-concept:C0012888,
umls-concept:C0014834,
umls-concept:C0020792,
umls-concept:C1167624,
umls-concept:C1314939,
umls-concept:C1548779,
umls-concept:C1947902,
umls-concept:C2827499
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pubmed:issue |
34
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pubmed:dateCreated |
1994-9-22
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pubmed:abstractText |
We have used two self-annealing template-primers (TPs) to covalently cross-link the Klenow fragment of Escherichia coli DNA polymerase I in its polymerase mode. The specificity of cross-linking is demonstrated by the observation that other template-primers, but not the template or primer alone, readily compete with self-annealing TPs. The enzyme-TP covalent complex is catalytically active and can incorporate one nucleotide on the primer terminus of the immobilized template-primer. Using a peptide mapping approach, we have identified a 17-amino acid tryptic peptide spanning residues 759-775 as a major constituent of the TP binding domain. Amino acid sequence analysis further revealed that Ile-765, Tyr-766 in the O-helix and Ser-769, Phe-771 in the O1-helix of the three-dimensional crystal structure of the Klenow fragment constitute the attachment site for TP.
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pubmed:grant |
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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/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonuclease V,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21828-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8063826-Affinity Labels,
pubmed-meshheading:8063826-Amino Acid Sequence,
pubmed-meshheading:8063826-Base Sequence,
pubmed-meshheading:8063826-Binding, Competitive,
pubmed-meshheading:8063826-Cations, Divalent,
pubmed-meshheading:8063826-Cross-Linking Reagents,
pubmed-meshheading:8063826-DNA Polymerase I,
pubmed-meshheading:8063826-DNA Primers,
pubmed-meshheading:8063826-DNA-Binding Proteins,
pubmed-meshheading:8063826-Dose-Response Relationship, Radiation,
pubmed-meshheading:8063826-Escherichia coli,
pubmed-meshheading:8063826-Exodeoxyribonuclease V,
pubmed-meshheading:8063826-Exodeoxyribonucleases,
pubmed-meshheading:8063826-Molecular Sequence Data,
pubmed-meshheading:8063826-Osmolar Concentration,
pubmed-meshheading:8063826-Peptide Fragments,
pubmed-meshheading:8063826-Sequence Analysis,
pubmed-meshheading:8063826-Trypsin,
pubmed-meshheading:8063826-Ultraviolet Rays
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pubmed:year |
1994
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pubmed:articleTitle |
Photoaffinity labeling of DNA template-primer binding site in Escherichia coli DNA polymerase I. Identification of involved amino acids.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry, New Jersey Medical School, Newark 07103.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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