title: Nucleoside triphosphate-dependent DNA-binding properties of mos protein.
abstract: We have previously shown that the mos gene product, p40mos, produced in Escherichia coli binds ATP and has ATPase activity. In the present study, we investigated the DNA-binding properties of p40mos and two mos deletion mutant proteins. Nitrocellulose blot protein-DNA binding assays showed that p40mos binds DNA in the presence of Mg2+-ATP and certain other nucleoside triphosphates. Ninety percent of the p40mos-bound DNA is dissociated if the complex is washed in the presence of 1 M NaCl or in the absence of ATP. p40mos-DNA binding is not observed in the presence of AMP or the nonhydrolyzable ATP analog adenosine 5'-[beta, gamma-methylene]-triphosphate; however, in the presence of ADP, p40mos binds DNA at 20% of the level that is observed with ATP. An N-terminal-deletion mutant protein, p19mos, has no DNA-binding activity, whereas a C-terminal-deletion mutant protein, p25mos, does. p25mos 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'-[beta, gamma-methylene]triphosphate, respectively. These results suggest that the N-terminal domain of p40mos is responsible for nucleoside triphosphate-mediated DNA binding. We also observed differential histone-DNA binding in the presence and absence of ATP.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D002872:Chromosome Deletion; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D007700:Kinetics; D009154:Mutation; D012265:Ribonucleotides / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012265:Ribonucleotides; D000255:Adenosine Triphosphate