Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (4)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Bryant, J. A.
Right arrow Articles by Anderson, L. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bryant, J. A.
Right arrow Articles by Anderson, L. E.
Agricola
Right arrow Articles by Bryant, J. A.
Right arrow Articles by Anderson, L. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Experimental Botany, Vol. 51, No. 352, pp. 1945-1947, November 1, 2000
© 2000 Oxford University Press

Short Communication

A novel DNA-binding protein associated with DNA polymerase-{alpha} in pea stimulates polymerase activity on infrequently primed templates

John A. Bryant1,3, David C. Brice1, Paul N. Fitchett1 and Louise E. Anderson2

1 School of Biological Sciences, University of Exeter, Exeter EX4 4QG, UK
2 Department of Biological Sciences, University of Illinois, Chicago, IL 60607-7060, USA

Abstract

A 42 kDa DNA-binding protein is associated with DNA polymerase-{alpha}-primase in pea (Pisum sativum). In a previous publication it was shown that the protein has strong preference for ds–ss junctions in DNA, including the cohesive termini generated by restriction endonucleases. In this paper it is shown that when the DNA-binding protein is added back to polymerase-primase, the protein stimulates the activity of the polymerase. The stimulation is particularly marked when M13 DNA, primed with a single sequencing primer or primed with oligoribonucleotides by the polymerase's associated primase activity, is used as a template. The stimulation of polymerase activity is not caused by an increase in processivity. These data lead to the suggestion that the 42 kDa DNA-binding protein is a primer-recognition protein.

Key words: DNA-binding protein, DNA polymerase, pea, Pisum sativum, primer, primer-recognition protein.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
D. E. Saslowsky, U. Warek, and B. S. J. Winkel
Nuclear Localization of Flavonoid Enzymes in Arabidopsis
J. Biol. Chem., June 24, 2005; 280(25): 23735 - 23740.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
D. C. Brice, J. A. Bryant, G. Dambrauskas, S. C. Drury, and J. A. Littlechild
Cloning and expression of cytosolic phosphoglycerate kinase from pea (Pisum sativum L.)
J. Exp. Bot., April 1, 2004; 55(398): 955 - 956.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
J. A. Bryant, K. Moore, and S. J. Aves
Origins and complexes: the initiation of DNA replication
J. Exp. Bot., February 1, 2001; 52(355): 193 - 202.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.