Identification of homologous pairing and strand-exchange activity from a human tumor cell line based on Z-DNA affinity chromatography.
AUTOR(ES)
Fishel, R A
RESUMO
An enzymatic activity that catalyzes ATP-dependent homologous pairing and strand exchange of duplex linear DNA and single-stranded circular DNA has been purified several thousand-fold from a human leukemic T-lymphoblast cell line. The activity was identified after chromatography of nuclear proteins on a Z-DNA column matrix. The reaction was shown to transfer the complementary single strand from a donor duplex linear substrate to a viral circular single-stranded acceptor beginning at the 5' end and proceeding in the 3' direction (5'----3'). Products of the strand-transfer reaction were characterized by electron microscopy. A 74-kDa protein was identified as the major ATP-binding peptide in active strand transferase fractions. The protein preparation described in this report binds more strongly to Z-DNA than to B-DNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=279476Documentos Relacionados
- recA protein promotes homologous-pairing and strand-exchange reactions between duplex DNA molecules.
- Occurrence of crossed strand-exchange forms in yeast DNA during meiosis.
- Crystal structure of a Z-DNA hexamer d(CGCICG) at 1.7 A resolution: inosine.cytidine base-pairing, and comparison with other Z-DNA structures.
- Optical absorption assay for strand-exchange reactions in unlabeled nucleic acids
- The effect of adriamycin on Z-DNA formation and DNA synthesis.
