- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Reha-Krantz, L. J.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Reha-Krantz, L. J.
Genetics, Vol 124, 213-220, Copyright © 1990
INVESTIGATIONS |
Genetic Evidence for Two Protein Domains and a Potential New Activity in Bacteriophage T4 DNA Polymerase
L. J. Reha-Krantz
Department of Genetics, University of Alberta, Edmonton, Alberta, Canada T6G 2E9
Intragenic complementation was detected within the bacteriophage T4 DNA polymerase gene. Complementation was observed between specific amino (N)-terminal, temperature-sensitive (ts) mutator mutants and more carboxy (C)-terminal mutants lacking DNA polymerase polymerizing functions. Protein sequences surrounding N-terminal mutation sites are similar to sequences found in Escherichia coli ribonuclease H (RNase H) and in the 5' -> 3' exonuclease domain of E. coli DNA polymerase I. These observations suggest that T4 DNA polymerase, like E. coli DNA polymerase I, contains a discrete N-terminal domain.
This article has been cited by other articles:
![]() |
E. S. Miller, E. Kutter, G. Mosig, F. Arisaka, T. Kunisawa, and W. Ruger Bacteriophage T4 Genome Microbiol. Mol. Biol. Rev., March 1, 2003; 67(1): 86 - 156. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y Ohya and D Botstein Diverse essential functions revealed by complementing yeast calmodulin mutants Science, February 18, 1994; 263(5149): 963 - 966. [Abstract] [PDF] |
||||

