PRIM2

From Wikipedia, the free encyclopedia

Primase, DNA, polypeptide 2 (58kDa)

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3L9Q, 3Q36, 4BPU, 4BPW, 4BPX

Identifiers

Symbols

PRIM2; PRIM2A; p58

External IDs

OMIM: 176636 MGI: 97758 HomoloGene: 731 GeneCards: PRIM2 Gene

EC number

2.7.7.-

Gene Ontology
Molecular function	• DNA binding • DNA primase activity • metal ion binding • 4 iron, 4 sulfur cluster binding
Cellular component	• nucleoplasm • replisome
Biological process	• G1/S transition of mitotic cell cycle • S phase of mitotic cell cycle • mitotic cell cycle • telomere maintenance via recombination • telomere maintenance • DNA replication, synthesis of RNA primer • DNA replication initiation • DNA strand elongation involved in DNA replication • telomere maintenance via semi-conservative replication
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
57.18 – 57.51 Mb

Chr 1:
33.45 – 33.67 Mb

PubMed search

DNA primase large subunit is an enzyme that in humans is encoded by the PRIM2 gene.^[1]^[2]

The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components. Primase, which is a heterodimer of a small subunit and a large subunit, synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. The protein encoded by this gene is the large, 58 kDa primase subunit.^[2]

References

↑ Shiratori A, Okumura K, Nogami M, Taguchi H, Onozaki T, Inoue T, Ando T, Shibata T, Izumi M, Miyazawa H, et al. (Feb 1996). "Assignment of the 49-kDa (PRIM1) and 58-kDa (PRIM2A and PRIM2B) subunit genes of the human DNA primase to chromosome bands 1q44 and 6p11.1-p12". Genomics 28 (2): 350–3. doi:10.1006/geno.1995.1155. PMID 8530050.
↑ 2.0 2.1 "Entrez Gene: PRIM2A primase, polypeptide 2A, 58kDa".

Stadlbauer F, Brueckner A, Rehfuess C, et al. (1994). "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase.". Eur. J. Biochem. 222 (3): 781–93. doi:10.1111/j.1432-1033.1994.tb18925.x. PMID 8026492.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Coll JM, Hickey RJ, Cronkey EA, et al. (1998). "Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome". Oncol. Res. 9 (11–12): 629–39. PMID 9563011.
Schneider A, Smith RW, Kautz AR, et al. (1998). "Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit". J. Biol. Chem. 273 (34): 21608–15. doi:10.1074/jbc.273.34.21608. PMID 9705292.
Arezi B, Kirk BW, Copeland WC, Kuchta RD (1999). "Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit". Biochemistry 38 (39): 12899–907. doi:10.1021/bi9908991. PMID 10504261.
Smith RW, Nasheuer HP (2002). "Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180". FEBS Lett. 527 (1–3): 143–6. doi:10.1016/S0014-5793(02)03197-6. PMID 12220650.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.

DNA replication (comparing Prokaryotic to Eukaryotic)

Initiation

Prokaryotic (initiation)	Pre-replication complex Cdc6 Helicase dnaA dnaB T7 Primase dnaG

Eukaryotic (preparation in G1 phase)	Pre-replication complex Origin recognition complex ORC1 ORC2 ORC3 ORC4 ORC5 ORC6 Cdc6 Cdt1 Minichromosome maintenance MCM2 MCM3 MCM4 MCM5 MCM6 MCM7 Licensing factor Autonomously replicating sequence Single-strand binding protein SSBP2 SSBP3 SSBP4 RNase H RNASEH1 RNASEH2A Helicase: HFM1 Primase: PRIM1 PRIM2

Both	Origin of replication/Ori/Replicon Replication fork Lagging and leading strands Okazaki fragment Primer

Replication

Prokaryotic (elongation)	DNA polymerase III holoenzyme dnaC dnaE dnaH dnaN dnaQ dnaT dnaX holA holB holC holD holE Replisome DNA ligase DNA clamp Topoisomerase DNA gyrase Prokaryotic DNA polymerase: DNA polymerase I Klenow fragment

Eukaryotic (synthesis in S phase)	Replication factor C RFC1 Flap endonuclease FEN1 Topoisomerase Replication protein A RPA1 Eukaryotic DNA polymerase: delta POLD1 POLD2 POLD3 POLD4 DNA clamp PCNA

Both	Movement: Processivity DNA ligase

Termination

Telomere: Telomerase
- TERT
- TERC
- DKC1

See also: DNA replication and repair-deficiency disorder B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.

PRIM2

References

Further reading