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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1995-1-17
|
| pubmed:abstractText |
The 57-kDa hepatic nuclear protein QUAD binds tightly and specifically a parallel tetrahelical form of the IgG switch region DNA (Weisman-Shomer, P. and Fry, M. (1993) J. Biol Chem. 268, 3306-3312). Here we show that QUAD is a heat-stable protein, maintaining approximately 90% of its tetrahelix binding activity after 10 min at 100 degrees C and becoming fully inactivated only after 30 min at 100 degrees C. To demonstrate that QUAD protects bound quadruplex DNA, naked and QUAD-bound tetrahelices were boiled, the protein residue in the complex was digested with trypsin and quadruplex and single-strand forms of the DNA component were resolved by electrophoresis. Whereas naked quadruplex DNA became fully denatured after 2 min at 100 degrees C, 55% of the QUAD-bound DNA was conserved as a tetrahelix after 6 min at 100 degrees C. These findings support the proposal that QUAD may act in vivo to stabilize tetrahelical DNA.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
205
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
305-11
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1994
|
| pubmed:articleTitle |
Stabilization of tetrahelical DNA by the quadruplex DNA binding protein QUAD.
|
| pubmed:affiliation |
Unit of Biochemistry, Bruce Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|