| pubmed-article:10856290 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10856290 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10856290 | lifeskim:mentions | umls-concept:C0165675 | lld:lifeskim |
| pubmed-article:10856290 | lifeskim:mentions | umls-concept:C0043481 | lld:lifeskim |
| pubmed-article:10856290 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:10856290 | pubmed:dateCreated | 2000-10-3 | lld:pubmed |
| pubmed-article:10856290 | pubmed:abstractText | Heterotrimeric human single-stranded DNA (ssDNA)-binding protein, replication protein A (RPA), is a central player in DNA replication, recombination, and repair. The C terminus of the largest subunit, RPA70, contains a putative zinc-binding motif and is implicated in complex formation with two smaller subunits, RPA14 and RPA32. The C-terminal domain of RPA70 (RPA70-CTD) was characterized using proteolysis and x-ray fluorescence emission spectroscopy. The proteolytic core of this domain comprised amino acids 432-616. X-ray fluorescence spectra revealed that RPA70-CTD possesses a coordinated Zn(II). The trimeric complex of RPA70-CTD, the ssDNA-binding domain of RPA32 (amino acids 43-171), and RPA14 had strong DNA binding activity. When properly coordinated with zinc, the trimer's affinity to ssDNA was only 3-10-fold less than that of the ssDNA-binding domain in the middle of RPA70. However, the DNA-binding activity of the trimer was dramatically reduced in the presence of chelating agents. Our data indicate that (i) Zn(II) is essential to stabilize the tertiary structure of RPA70-CTD; (ii) RPA70-CTD possesses DNA-binding activity, which is modulated by Zn(II); and (iii) ssDNA binding by the trimer is a synergistic effect generated by the RPA70-CTD and RPA32. | lld:pubmed |
| pubmed-article:10856290 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10856290 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10856290 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10856290 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10856290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10856290 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10856290 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10856290 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10856290 | pubmed:author | pubmed-author:KorolevSS | lld:pubmed |
| pubmed-article:10856290 | pubmed:author | pubmed-author:BochkarevAA | lld:pubmed |
| pubmed-article:10856290 | pubmed:author | pubmed-author:BochkarevaEE | lld:pubmed |
| pubmed-article:10856290 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10856290 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10856290 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10856290 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10856290 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10856290 | pubmed:pagination | 27332-8 | lld:pubmed |
| pubmed-article:10856290 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10856290 | pubmed:meshHeading | pubmed-meshheading:10856290... | lld:pubmed |
| pubmed-article:10856290 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10856290 | pubmed:articleTitle | The role for zinc in replication protein A. | lld:pubmed |
| pubmed-article:10856290 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, the University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190, USA. | lld:pubmed |
| pubmed-article:10856290 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10856290 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10856290 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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