DNA unwinding protein from meiotic cells of Lilium
- 1 May 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (10) , 1872-1880
- https://doi.org/10.1021/bi00603a011
Abstract
An ATP-dependent DNA unwinding protein is present at a high level of activity in meiotic cells of lilies. The protein also acts as a DNA-dependent ATPase, the single strand form being the preferred cofactor. It binds in the absence of ATP to single-strand DNA and to ends or nicks in duplex DNA. A 3''-OH terminus is required for binding at duplex ends; such binding is highly stable. Unwinding occurs in the presence of ATP, and it is limited to about 50 base pairs per end or 400-500 base pairs per nick. The ATP hydrolyzed during unwinding is distinguishable from ATP hydrolysis in the presence of single-strand DNA.This publication has 9 references indexed in Scilit:
- A phosphorylatable DNA-binding protein associated with a lipoprotein fraction from rat spermatocyte nuclei*1Experimental Cell Research, 1977
- DNA Unwinding Enzyme II of Escherichia coliEuropean Journal of Biochemistry, 1977
- DNA Unwinding Enzyme II of Escherichia coliEuropean Journal of Biochemistry, 1977
- Enzymatic unwinding of DNAJournal of Molecular Biology, 1977
- A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: catalytic strand separation in advance of replication.Proceedings of the National Academy of Sciences, 1977
- On the existence of polyadenylated histone mRNA in Xenopus laevis oocytesCell, 1976
- Enzymic Unwinding of DNAEuropean Journal of Biochemistry, 1976
- Enzymic Unwinding of DNAEuropean Journal of Biochemistry, 1976
- MOLECULAR SIZE AND CIRCULARITY OF DNA IN CELLS OF MAMMALS AND HIGHER PLANTSProceedings of the National Academy of Sciences, 1965