PRI1/YIR008C Summary Help

PRI1 BASIC INFORMATION

Standard Name PRI1
Systematic Name YIR008C
Feature Type ORF, Verified
Description Subunit of DNA primase, which is required for DNA synthesis and double-strand break repair (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description DNA PRImase
GO Annotations All PRI1 GO evidence and references
    View Computational GO annotations for PRI1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All PRI1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions PRI1 All interactions details and references
155 total interaction(s) for 137 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 15
  • Affinity Capture-Western: 1
  • Co-localization: 2
  • Co-purification: 3
  • Reconstituted Complex: 1
Genetic Interactions
  • Phenotypic Enhancement: 76
  • Phenotypic Suppression: 47
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 9
Sequence Information
ChrIX:374303 to 373074 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 1994-12-10 | Sequence: 1994-12-10
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1230 374303..373074 1994-12-10 1994-12-10
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000001447

PRI1 RESOURCES

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SGD ORF map
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  • Localization Resources
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for PRI1

SUMMARY PARAGRAPH for PRI1

PRI1 is an essential gene (1); it encodes the smallest subunit of DNA polymerase alpha (6), formerly called DNA polymerase I (7); reviewed in 3, 8; also see 6). Yeast DNA polymerase alpha comprises four subunits, of MW 167 kD (Pol1p), 79 kD (Pol12p), 62 kD (Pri2p), and 48 kD (Pri1p). Polymerase alpha is required for DNA replication; it is invloved both in initiation and in priming Okazaki fragments during lagging strand elongation. It has no associated proofreading exonuclease activity; the two smaller subunits form the primase activity that synthesizes short RNA primers in DNA replication. Purified Pri1p is sufficient to synthesize RNA primers on a DNA template, although primer extension in more efficient in the presence of Pri2p 2. In yeast, DNA polymerase alpha activity is required for premeiotic DNA replication and sporulation and for double-strand break repair (9), but not for other DNA repair synthesis (10, 11).

DNA primase may also couple DNA replication to the DNA damage checkpoint. A mutation in MEC3, which encodes a DNA damage checkpoint protein, can suppress the cold sensitivity of the pri1-2 mutant (12). Another mutation in PRI1, pri1-M4, causes sensitivity to DNA damaging agents and a defect in the G1-S phase DNA damage response (13).

Conditional mutations in PRI1 show altered DNA synthesis at the restrictive temperature (14), as well as increased mitotic intrachromosomal recombination and spontaneous mutation rates (15).

Like many other genes encoding DNA replication proteins, PRI1 is transcribed during late G1 and S phases of the cell cycle (16); however, all four subunits of polymerase alpha are present in a complex throughout the cell cycle (17).FU,PI, Though the mouse Pri1p homolog is very similar to the yeast protein, it cannot complement a pri1 mutation (18).

Last updated: 1999-05-07

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for PRI1]

1) Lucchini G, et al.  (1987) Yeast DNA polymerase--DNA primase complex; cloning of PRI 1, a single essential gene related to DNA primase activity. EMBO J 6(3):737-42
2) Santocanale C, et al.  (1993) The isolated 48,000-dalton subunit of yeast DNA primase is sufficient for RNA primer synthesis. J Biol Chem 268(2):1343-8
3) Burgers PM  (1998) Eukaryotic DNA polymerases in DNA replication and DNA repair. Chromosoma 107(4):218-27
4) Brooke RG and Dumas LB  (1991) Reconstitution of the Saccharomyces cerevisiae DNA primase-DNA polymerase protein complex in vitro. The 86-kDa subunit facilitates but is not required for complex formation. J Biol Chem 266(16):10093-8
5) Biswas SB, et al.  (2003) Subunit interactions in the assembly of Saccharomyces cerevisiae DNA polymerase alpha. Nucleic Acids Res 31(8):2056-65
6) Plevani P, et al.  (1988) The yeast DNA polymerase-primase complex: genes and proteins. Biochim Biophys Acta 951(2-3):268-73
7) Burgers PM, et al.  (1990) Revised nomenclature for eukaryotic DNA polymerases. Eur J Biochem 191(3):617-8
8) Sugino A  (1995) Yeast DNA polymerases and their role at the replication fork. Trends Biochem Sci 20(8):319-23
9) Holmes AM and Haber JE  (1999) Double-strand break repair in yeast requires both leading and lagging strand DNA polymerases. Cell 96(3):415-24
10) Budd ME, et al.  (1989) DNA polymerase I is required for premeiotic DNA replication and sporulation but not for X-ray repair in Saccharomyces cerevisiae. Mol Cell Biol 9(2):365-76
11) Wang Z, et al.  (1993) DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase epsilon and is influenced by DNA polymerases alpha and delta in Saccharomyces cerevisiae. Mol Cell Biol 13(2):1051-8
12) Longhese MP, et al.  (1996) Yeast pip3/mec3 mutants fail to delay entry into S phase and to slow DNA replication in response to DNA damage, and they define a functional link between Mec3 and DNA primase. Mol Cell Biol 16(7):3235-44
13) Marini F, et al.  (1997) A role for DNA primase in coupling DNA replication to DNA damage response. EMBO J 16(3):639-50
14) Francesconi S, et al.  (1991) Mutations in conserved yeast DNA primase domains impair DNA replication in vivo. Proc Natl Acad Sci U S A 88(9):3877-81
15) Longhese MP, et al.  (1993) Conditional mutations in the yeast DNA primase genes affect different aspects of DNA metabolism and interactions in the DNA polymerase alpha-primase complex. Genetics 133(2):183-91
16) Johnston LH, et al.  (1990) Expression of the yeast DNA primase gene, PRI1, is regulated within the mitotic cell cycle and in meiosis. Mol Gen Genet 221(1):44-8
17) Ferrari M, et al.  (1996) Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide. J Biol Chem 271(15):8661-6
18) Santocanale C, et al.  (1992) Overproduction and functional analysis of DNA primase subunits from yeast and mouse. Gene 113(2):199-205