We characterized and purified an acidic dATP-binding protein, which, in its active form, resides in the nuclear fraction of a range of cells from mammals (including pig liver) and baker's yeast (Saccharomyces cerevisiae). This protein exhibits a high degree of specificity for the deoxy form of the naturally occurring nucleoside triphosphates and shows a marked preference for the purine deoxynucleoside triphosphates dATP and dGTP. The protein cleaves the terminal phosphate of dATP and appears to retain the dADP moiety of the nucleotide in a reaction that is resistant to both SDS and 8 M-urea. Fractionation of the nuclear preparation followed by non-denaturing PAGE and SDS/PAGE electrophoresis was sufficient to produce pure protein. The occurrence of this activity in all nuclei tested suggests that it plays an important role in nuclear metabolism. The specificity of the enzyme for deoxynucleoside triphosphates further suggests a role for this enzyme in DNA replication or repair, but the acidity of the protein argues against a direct interaction with DNA, and, indeed, the catalytic activity is not modulated by the inclusion of DNA in a variety of physical forms.
Skip Nav Destination
Article navigation
November 1992
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkAdvertising
Research Article|
November 01 1992
Characterization and purification of a novel dATP-binding protein in eukaryotes
A Dalton;
A Dalton
*Department of Molecular Biology and Biotechnology.
Search for other works by this author on:
D P Hornby;
D P Hornby
*Department of Molecular Biology and Biotechnology.
Search for other works by this author on:
S P Langston;
S P Langston
†Department of Chemistry, Krebs Institute, University of Sheffield, Sheffield S1O 2TN, U.K.
Search for other works by this author on:
G M Blackburn
G M Blackburn
†Department of Chemistry, Krebs Institute, University of Sheffield, Sheffield S1O 2TN, U.K.
Search for other works by this author on:
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1992 The Biochemical Society, London
1992
Biochem J (1992) 287 (3): 871–879.
Citation
A Dalton, D P Hornby, S P Langston, G M Blackburn; Characterization and purification of a novel dATP-binding protein in eukaryotes. Biochem J 1 November 1992; 287 (3): 871–879. doi: https://doi.org/10.1042/bj2870871
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.