title: DNA and ATP binding activities of the baculovirus DNA helicase P143.
abstract: P143 is a DNA helicase that tightly binds both double-stranded and single-stranded DNA. DNA-protein complexes rapidly dissociated in the presence of ATP and Mg(2+). This finding suggests that ATP hydrolysis causes a conformational change in P143 which decreases affinity for DNA. This supports the model of an inchworm mechanism of DNA unwinding.
authors: Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128, USA.
authors: V V
authors: VV
authors: McDougal
authors: L A
authors: LA
authors: Guarino
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002413:Cations, Divalent; D004247:DNA / Q000378:metabolism*; D004265:DNA Helicases / Q000378:metabolism*; D006868:Hydrolysis; D008958:Models, Molecular; D009036:Moths / Q000821:virology; D017924:Nucleopolyhedroviruses / Q000201:enzymology*; D011485:Protein Binding
chemical_list: D002413:Cations, Divalent; D000255:Adenosine Triphosphate; D004247:DNA; D004265:DNA Helicases