Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
1996-5-28
|
pubmed:abstractText |
We have identified a series of proteins with an affinity for cisplatin -damaged DNA using damaged DNA affinity chromatography. We have purified one of these proteins to homogeneity on the basis of a mobility shift assay detecting binding to cisplatin-damaged DNA. The protein was identified as high-mobility group 1 protein (HMG-1) by N-terminal protein sequence analysis. Analysis of a variety of DNA structures revealed that fully duplex DNAs were the best substrates for HMG-1 binding, while partial duplexes were less avidly bound. The decreased levels of binding are attributed to the length of the duplex region of the DNA substrates. A 3-fold increase in binding was observed when a cisplatin-damaged DNA substrate containing a single break in the phosphodiester backbone was joined by DNA ligase. The strict DNA size dependence of binding was also assessed, and a 10-fold increase in binding was observed when the length of the DNA duplex was increased from 44 to 180 base pairs (bp) at the same level of cisplatin damage. HMG-1 binding also was correlated with the degree of cisplatin-DNA damage, suggesting a higher affinity for DNA containing multiple cisplatin adducts. Nuclease degradation of the cisplatin-damaged DNA demonstrated that at the lowest levels of cisplatin damage all of the substrates contained at least one cisplatin adduct. The potential role of HMG-1 in the repair of cisplatin-DNA adducts is discussed.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cisplatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Adducts,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/cisplatin-DNA adduct
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
35
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2992-3000
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:8608137-Animals,
pubmed-meshheading:8608137-Base Sequence,
pubmed-meshheading:8608137-Cattle,
pubmed-meshheading:8608137-Chromatography, Gel,
pubmed-meshheading:8608137-Cisplatin,
pubmed-meshheading:8608137-DNA Adducts,
pubmed-meshheading:8608137-DNA Repair,
pubmed-meshheading:8608137-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8608137-High Mobility Group Proteins,
pubmed-meshheading:8608137-Humans,
pubmed-meshheading:8608137-Kinetics,
pubmed-meshheading:8608137-Molecular Sequence Data,
pubmed-meshheading:8608137-Molecular Weight,
pubmed-meshheading:8608137-Oligodeoxyribonucleotides,
pubmed-meshheading:8608137-Substrate Specificity,
pubmed-meshheading:8608137-Thymus Gland
|
pubmed:year |
1996
|
pubmed:articleTitle |
Cisplatin-DNA binding specificity of calf high-mobility group 1 protein.
|
pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Wright State University, Dayton, Ohio 45435, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|