Mutational studies of human DNA polymerase alpha. Serine 867 in the second most conserved region among alpha-like DNA polymerases is involved in primer binding and mispair primer extension.
Open Access
- 1 November 1993
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (32) , 24175-24182
- https://doi.org/10.1016/s0021-9258(20)80507-9
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Catalytic subunit of human DNA polymerase alpha overproduced from baculovirus-infected insect cells. Structural and enzymological characterization.Journal of Biological Chemistry, 1991
- Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopyBiochemistry, 1991
- Human DNA polymerase α catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminusNucleic Acids Research, 1990
- A third essential DNA polymerase in S. cerevisiaeCell, 1990
- Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli.Journal of Biological Chemistry, 1990
- Linearization of baculovirus DNA enhances the recovery of recombinant virus expression vectorsNucleic Acids Research, 1990
- An attempt to unify the structure of polymerasesProtein Engineering, Design and Selection, 1990
- DNA replication fidelity: kinetics and thermodynamicsMutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 1988
- Rapid and efficient site-specific mutagenesis without phenotypic selection.Proceedings of the National Academy of Sciences, 1985
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976