Biochemical Analyses of Mutations in the HSV-1 Helicase-Primase That Alter ATP Hydrolysis, DNA Unwinding, and Coupling Between Hydrolysis and Unwinding
Open Access
- 1 February 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (7) , 4623-4630
Abstract
No abstract availableKeywords
This publication has 66 references indexed in Scilit:
- Biochemical Analysis of Mutant T7 Primase/Helicase Proteins Defective in DNA Binding, Nucleotide Hydrolysis, and the Coupling of Hydrolysis with DNA UnwindingJournal of Biological Chemistry, 1996
- Lysine 71 of the Chaperone Protein Hsc70 Is Essential for ATP HydrolysisJournal of Biological Chemistry, 1996
- DNA Helicases: New Breeds of Translocating Motors and Molecular PumpsCell, 1996
- Hexameric Rings of Escherichia coli RuvB Protein.Journal of Molecular Biology, 1994
- Helicase Motifs V and VI of the Escherichia coli UvrB Protein of the UvrABC Endonuclease Are Essential for the Formation of the Preincision ComplexJournal of Molecular Biology, 1994
- A Dominant Negative Allele of the Escherichia coli uvrD Gene Encoding DNA Helicase IIJournal of Molecular Biology, 1994
- DNA-induced dimerization of the Escherichia coli Rep helicaseJournal of Molecular Biology, 1991
- ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replicationNature, 1989
- A novel superfamily of nucleoside triphosphate‐binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombinationFEBS Letters, 1988
- Stabilization of the hexameric form of Escherichia coli protein rho under ATP hydrolysis conditionsJournal of Molecular Biology, 1982