- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Email this article to a friend
- 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 Longhese, M. P.
- Articles by Lucchini, G.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Longhese, M. P.
- Articles by Lucchini, G.
Genetics, Vol 133, 183-191, Copyright © 1993
INVESTIGATIONS |
Conditional Mutations in the Yeast DNA Primase Genes Affect Different Aspects of DNA Metabolism and Interactions in the DNA Polymerase {alpha}-Primase Complex
M. P. Longhese, L. Jovine, P. Plevani and G. Lucchini
Dipartimento di Genetica e di Biologia dei Microrganismi, Universita di Milano, 20133 Milano, Italy
Different pri1 and pri2 conditional mutants of Saccharomyces cerevisiae altered, respectively, in the small (p48) and large (p58) subunits of DNA primase, show an enhanced rate of both mitotic intrachromosomal recombination and spontaneous mutation, to an extent which is correlated with the severity of their defects in cell growth and DNA synthesis. These effects might be attributable to the formation of nicked and gapped DNA molecules that are substrates for recombination and error-prone repair, due to defective DNA replication in the primase mutants. Furthermore, pri1 and pri2 mutations inhibit sporulation and affect spore viability, with the unsporulated mutant cells arresting with a single nucleus, suggesting that DNA primase plays a critical role during meiosis. The observation that all possible pairwise combinations of two pri1 and two pri2 alleles are lethal provides further evidence for direct interaction of the primase subunits in vivo. Immunopurification and immunoprecipitation studies on wild-type and mutant strains suggest that the small subunit has a major role in determining primase activity, whereas the large subunit directly interacts with DNA polymerase {alpha}, and either mediates or stabilizes association of the p48 polypeptide in the DNA polymerase {alpha}-primase complex.
This article has been cited by other articles:
 |
|
 |
|
  B. E. Weiner, H. Huang, B. M. Dattilo, M. J. Nilges, E. Fanning, and W. J. Chazin An Iron-Sulfur Cluster in the C-terminal Domain of the p58 Subunit of Human DNA Primase J. Biol. Chem., November 16, 2007; 282(46): 33444 - 33451. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Ofir, S. Sagee, N. Guttmann-Raviv, L. Pnueli, and Y. Kassir The Role and Regulation of the preRC Component Cdc6 in the Initiation of Premeiotic DNA Replication Mol. Biol. Cell, May 1, 2004; 15(5): 2230 - 2242. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Lottersberger, F. Rubert, V. Baldo, G. Lucchini, and M. P. Longhese Functions of Saccharomyces cerevisiae 14-3-3 Proteins in Response to DNA Damage and to DNA Replication Stress Genetics, December 1, 2003; 165(4): 1717 - 1732. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Mizuno, K. Yamagishi, H. Miyazawa, and F. Hanaoka Molecular Architecture of the Mouse DNA Polymerase alpha -Primase Complex Mol. Cell. Biol., November 1, 1999; 19(11): 7886 - 7896. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Ferrari, G. Lucchini, P. Plevani, and M. Foiani Phosphorylation of the DNA Polymerase alpha-Primase B Subunit Is Dependent on Its Association with the p180 Polypeptide J. Biol. Chem., April 12, 1996; 271(15): 8661 - 8666. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T Mizuno, T Okamoto, M Yokoi, M Izumi, A Kobayashi, T Hachiya, K Tamai, T Inoue, and F Hanaoka Identification of the nuclear localization signal of mouse DNA primase: nuclear transport of p46 subunit is facilitated by interaction with p54 subunit J. Cell Sci., January 11, 1996; 109(11): 2627 - 2636. [Abstract] [PDF]
|
|
|
|
|
|
W. C. Copeland and X. Tan Active Site Mapping of the Catalytic Mouse Primase Subunit by Alanine Scanning Mutagenesis J. Biol. Chem., February 24, 1995; 270(8): 3905 - 3913. [Abstract] [Full Text] [PDF]
|
|