Nucleoside triphosphate-dependent DNA-binding properties of mos protein

A. Seth, E. Priel, G. F. Vande Woude

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3 Scopus citations


We have previously shown that the mos gene product, p40(mos), produced in Escherichia coli binds ATP and has ATPase activity. In the present study, we investigated the DNA-binding properties of p40(mos) and two mos deletion mutant proteins. Nitrocellulose blot protein-DNA binding assays showed that p40(mos) binds DNA in the presence of Mg2+-ATP and certain other nucleoside triphosphates. Ninety percent of the p40(mos)-bound DNA is dissociated if the complex is washed in the presence of 1 M NaCl or in the absence of ATP. p40(mos)-DNA binding is not observed in the presence of AMP or the nonhydrolyzable ATP analog adenosine 5'-[β,γ-methylene]triphosphate; however, in the presence of ADP, p40(mos) binds DNA at 20% of the level that is observed with ATP. An N-terminal-deletion mutant protein, p19(mos), has no DNA-binding activity, whereas a C-terminal-deletion mutant protein, p25(mos), does. p25(mos) contains the ATP-binding domain, binds DNA in the presence of either ADP or ATP, and shows 5% and 45% binding (relative to that in the presence of ATP) in the presence of AMP and adenosine 5'-[β,γ-methylene]triphosphate, respectively. These results suggest that the N-terminal domain of p40(mos) is responsible for nucleoside triphosphate-mediated DNA binding. We also observed differential histone-DNA binding in the presence and absence of ATP.

Original languageEnglish
Pages (from-to)3560-3564
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number11
StatePublished - 1 Jan 1987
Externally publishedYes

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