PRIM2

PRIM2

Primase, polypeptide 2A, 58kDa, also known as PRIM2A, is a human gene.

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PRIM2A primase, polypeptide 2A, 58kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5558| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Stadlbauer F, Brueckner A, Rehfuess C, "et al." |title=DNA replication in vitro by recombinant DNA-polymerase-alpha-primase. |journal=Eur. J. Biochem. |volume=222 |issue= 3 |pages= 781–93 |year= 1994 |pmid= 8026492 |doi=10.1111/j.1432-1033.1994.tb18925.x
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8
*cite journal | author=Shiratori A, Okumura K, Nogami M, "et al." |title=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. |journal=Genomics |volume=28 |issue= 2 |pages= 350–3 |year= 1996 |pmid= 8530050 |doi=10.1006/geno.1995.1155
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3
*cite journal | author=Coll JM, Hickey RJ, Cronkey EA, "et al." |title=Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome. |journal=Oncol. Res. |volume=9 |issue= 11-12 |pages= 629–39 |year= 1998 |pmid= 9563011 |doi=
*cite journal | author=Schneider A, Smith RW, Kautz AR, "et al." |title=Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 21608–15 |year= 1998 |pmid= 9705292 |doi=10.1074/jbc.273.34.21608
*cite journal | author=Arezi B, Kirk BW, Copeland WC, Kuchta RD |title=Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit. |journal=Biochemistry |volume=38 |issue= 39 |pages= 12899–907 |year= 1999 |pmid= 10504261 |doi=10.1021/bi9908991
*cite journal | author=Smith RW, Nasheuer HP |title=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. |journal=FEBS Lett. |volume=527 |issue= 1-3 |pages= 143–6 |year= 2002 |pmid= 12220650 |doi=10.1016/S0014-5793(02)03197-6
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Mungall AJ, Palmer SA, Sims SK, "et al." |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rush J, Moritz A, Lee KA, "et al." |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем сделать НИР

Look at other dictionaries:

  • prim — PRIM1, primuri, s.n. (reg.) Garnitură din blană (neagră, de miel) aplicată pe marginea căciulilor, a pieptarelor, a hainelor. – Din magh. prém. Trimis de ana zecheru, 30.03.2008. Sursa: DEX 98  PRIM2, Ă, primi, e, num. ord. (Adesea cu valoare de …   Dicționar Român

  • DNA ligase — repairing chromosomal damage Identifiers EC number 6.5.1.1 …   Wikipedia

  • DNA replication — DNA replication. The double helix is unwound and each strand acts as a template for the next strand. Bases are matched to synthesize the new partner strands. DNA replication is a biological process that occurs in all living organisms and copies… …   Wikipedia

  • Polymerase — Structure of Taq DNA polymerase A polymerase (EC 2.7.7.6/7/19/48/49) is an enzyme whose central function is associated with polymers of nucleic acids such as RNA and DNA. The primary function of a polymerase is the polymerization of new DNA or… …   Wikipedia

  • Primer (molecular biology) — A primer is a strand of nucleic acid that serves as a starting point for DNA synthesis. They are required for DNA replication because the enzymes that catalyze this process, DNA polymerases, can only add new nucleotides to an existing strand of… …   Wikipedia

  • DNA polymerase — 3D structure of the DNA binding helix turn helix motifs in human DNA polymerase beta A DNA polymerase is an enzyme that helps catalyze in the polymerization of deoxyribonucleotides into a DNA strand. DNA polymerases are best known for their… …   Wikipedia

  • Topoisomerase — Topoisomerases (type I: EC 5.99.1.2, type II: EC 5.99.1.3) are enzymes that regulate the overwinding or underwinding of DNA. The winding problem of DNA arises due to the intertwined nature of its double helical structure. For example, during DNA… …   Wikipedia

  • Primase — DNA primase is an enzyme involved in the replication of DNA. Primase catalyzes the synthesis of a short RNA (or DNA in some organisms [1]) segment called a primer complementary to a ssDNA template. Primase is of key importance in DNA replication… …   Wikipedia

  • Helicase — Structure of E. coli helicase RuvA Helicases are a class of enzymes vital to all living organisms. They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands (i.e.,… …   Wikipedia

  • DNA polymerase I — Functional domains in the Klenow Fragment (left) and DNA Polymerase I (right). DNA Polymerase I (or Pol I) is an enzyme that participates in the process of DNA replication in prokaryotes. It is composed of 928 amino acids, and is an example of a… …   Wikipedia

Share the article and excerpts

Direct link
… Do a right-click on the link above
and select “Copy Link”