Faktor licenciranja DNK replikacije MCM3

edit
Komponenta 3 kompleksa minihromozomskog održavanja
Identifikatori
SimboliMCM3; HCC5; P1-MCM3; P1.h; RLFB
Vanjski IDOMIM: 602693 MGI: 101845 HomoloGene: 1791 GeneCards: MCM3 Gene
EC broj3.6.4.12
Ontologija gena
Molekulska funkcija DNK vezivanje
aktivnosti DNK helikaze
vezivanje za mesto početka DNK replikacije
Ćelijska komponenta hromatin
nukleus
nukleoplazma
Biološki proces kontrolna tačka ćelijskog ciklusa
G1/S tranzicija mitotičkog ćelijskog ciklusa
S faza mitotičkog ćelijskog ciklusa
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez417217215
EnsemblENSG00000112118ENSMUSG00000041859
UniProtP25205P25206
Ref. Sekv. (iRNK)NM_001270472NM_008563
Ref. Sekv. (protein)NP_001257401NP_032589
Lokacija (UCSC)Chr 6:
52.13 - 52.15 Mb
Chr 1:
20.8 - 20.82 Mb
PubMed pretraga[1][2]

Faktor licenciranja DNK replikacije MCM3 je protein koji je kod ljudi kodiran MCM3 genom.[1]

Protein kodiran ovim genom je jedan od visoko konzerviranjih proteina održavanja mini-hromozoma (MCM) koji učestvuju u inicijaciji replikacije eukariotskog genoma. Heksamerni proteinski kompleks formiran od MCM proteina je ključna komponenta prereplikacionog kompleksa (pre-RC). On učestuje u formiranju replikacionih viljuški i regrutaciji drugih srodnih proteina replikacije DNK. Ovaj protein formira kompleks sa MCM4, 6, i 7, i pokazano je da reguliše helikaznu aktivnost kompleksa. On direktno dolazi u kontakt sa MCM5/CDC46. Ovaj protein formira interakcije, i biva acetilisan posredstvom MCM3AP, acetiltransferaze asocirane sa hromatinom. Acetilacija ovog proteina inhibira inicijaciju DNK replikacije i progresiju ćelijskog ciklusa.[2]

Interakcije

MCM3 formira interakcije sa ORC4L,[3] ORC5L,[3] CDC6,[4][5] MCM3AP,[6][7][8] MCM5,[3][9] MCM7,[3][4][10][11] DBF4,[3] MCM2[3] i CDC45-srodan protein.[3]

Reference

  1. Thommes P, Fett R, Schray B, Burkhart R, Barnes M, Kennedy C, Brown NC, Knippers R (April 1992). „Properties of the nuclear P1 protein, a mammalian homologue of the yeast Mcm3 replication protein”. Nucleic Acids Res 20 (5): 1069–74. DOI:10.1093/nar/20.5.1069. PMC 312092. PMID 1549468. 
  2. „Entrez Gene: MCM3 MCM3 minichromosome maintenance deficient 3 (S. cerevisiae)”. 
  3. 3,0 3,1 3,2 3,3 3,4 3,5 3,6 Kneissl, Margot; Pütter Vera, Szalay Aladar A, Grummt Friedrich (March 2003). „Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells”. J. Mol. Biol. (England) 327 (1): 111–28. DOI:10.1016/S0022-2836(03)00079-2. ISSN 0022-2836. PMID 12614612. 
  4. 4,0 4,1 Fujita, M; Yamada C, Goto H, Yokoyama N, Kuzushima K, Inagaki M, Tsurumi T (September 1999). „Cell cycle regulation of human CDC6 protein. Intracellular localization, interaction with the human mcm complex, and CDC2 kinase-mediated hyperphosphorylation”. J. Biol. Chem. (UNITED STATES) 274 (36): 25927–32. DOI:10.1074/jbc.274.36.25927. ISSN 0021-9258. PMID 10464337. 
  5. Méndez, J; Stillman B (November 2000). „Chromatin Association of Human Origin Recognition Complex, Cdc6, and Minichromosome Maintenance Proteins during the Cell Cycle: Assembly of Prereplication Complexes in Late Mitosis”. Mol. Cell. Biol. (UNITED STATES) 20 (22): 8602–12. DOI:10.1128/MCB.20.22.8602-8612.2000. ISSN 0270-7306. PMC 102165. PMID 11046155. 
  6. Takei, Yoshinori; Assenberg Magdalena, Tsujimoto Gozoh, Laskey Ronald (November 2002). „The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of DNA replication via interaction with MCM3”. J. Biol. Chem. (United States) 277 (45): 43121–5. DOI:10.1074/jbc.C200442200. ISSN 0021-9258. PMID 12226073. 
  7. Kuwahara, K; Yoshida M, Kondo E, Sakata A, Watanabe Y, Abe E, Kouno Y, Tomiyasu S, Fujimura S, Tokuhisa T, Kimura H, Ezaki T, Sakaguchi N (April 2000). „A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of the germinal center and associated with MCM3, a protein essential for DNA replication”. Blood (UNITED STATES) 95 (7): 2321–8. ISSN 0006-4971. PMID 10733502. 
  8. Takei, Y; Tsujimoto G (August 1998). „Identification of a novel MCM3-associated protein that facilitates MCM3 nuclear localization”. J. Biol. Chem. (UNITED STATES) 273 (35): 22177–80. DOI:10.1074/jbc.273.35.22177. ISSN 0021-9258. PMID 9712829. 
  9. DaFonseca, C J; Shu F, Zhang J J (March 2001). „Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-γ”. Proc. Natl. Acad. Sci. U.S.A. (United States) 98 (6): 3034–9. DOI:10.1073/pnas.061487598. ISSN 0027-8424. PMC 30602. PMID 11248027. 
  10. Fujita, M; Kiyono T, Hayashi Y, Ishibashi M (April 1997). „In vivo interaction of human MCM heterohexameric complexes with chromatin. Possible involvement of ATP”. J. Biol. Chem. (UNITED STATES) 272 (16): 10928–35. DOI:10.1074/jbc.272.16.10928. ISSN 0021-9258. PMID 9099751. 
  11. Fujita, Masatoshi; Ishimi Yukio, Nakamura Hiromu, Kiyono Tohru, Tsurumi Tatsuya (March 2002). „Nuclear organization of DNA replication initiation proteins in mammalian cells”. J. Biol. Chem. (United States) 277 (12): 10354–61. DOI:10.1074/jbc.M111398200. ISSN 0021-9258. PMID 11779870. 

Literatura

  • Musahl C, Schulte D, Burkhart R, Knippers R (1995). „A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins”. Eur. J. Biochem. 230 (3): 1096–101. DOI:10.1111/j.1432-1033.1995.tb20660.x. PMID 7601140. 
  • Schulte D, Burkhart R, Musahl C, et al. (1995). „Expression, phosphorylation and nuclear localization of the human P1 protein, a homologue of the yeast Mcm 3 replication protein”. J. Cell. Sci. 108 (4): 1381–9. PMID 7615659. 
  • Starborg M, Brundell E, Gell K, et al. (1995). „A murine replication protein accumulates temporarily in the heterochromatic regions of nuclei prior to initiation of DNA replication”. J. Cell. Sci. 108 (3): 927–34. PMID 7622621. 
  • Burkhart R, Schulte D, Hu D, et al. (1995). „Interactions of human nuclear proteins P1Mcm3 and P1Cdc46”. Eur. J. Biochem. 228 (2): 431–8. DOI:10.1111/j.1432-1033.1995.tb20281.x. PMID 7705359. 
  • Kubota Y, Mimura S, Nishimoto S, et al. (1995). „Identification of the yeast MCM3-related protein as a component of Xenopus DNA replication licensing factor”. Cell 81 (4): 601–9. DOI:10.1016/0092-8674(95)90081-0. PMID 7758114. 
  • Madine MA, Khoo CY, Mills AD, Laskey RA (1995). „MCM3 complex required for cell cycle regulation of DNA replication in vertebrate cells”. Nature 375 (6530): 421–4. DOI:10.1038/375421a0. PMID 7760938. 
  • 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. 
  • Hu B, Burkhart R, Schulte D, et al. (1994). „The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins”. Nucleic Acids Res. 21 (23): 5289–93. DOI:10.1093/nar/21.23.5289-a. PMC 310560. PMID 8265339. 
  • Schulte D, Richter A, Burkhart R, et al. (1996). „Properties of the human nuclear protein p85Mcm. Expression, nuclear localization and interaction with other Mcm proteins”. Eur. J. Biochem. 235 (1–2): 144–51. DOI:10.1111/j.1432-1033.1996.00144.x. PMID 8631321. 
  • Ishimi Y, Ichinose S, Omori A, et al. (1996). „Binding of human minichromosome maintenance proteins with histone H3”. J. Biol. Chem. 271 (39): 24115–22. DOI:10.1074/jbc.271.39.24115. PMID 8798650. 
  • Sato N, Arai K, Masai H (1997). „Human and Xenopus cDNAs encoding budding yeast Cdc7-related kinases: in vitro phosphorylation of MCM subunits by a putative human homologue of Cdc7”. EMBO J. 16 (14): 4340–51. DOI:10.1093/emboj/16.14.4340. PMC 1170060. PMID 9250678. 
  • 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. 
  • Takei Y, Tsujimoto G (1998). „Identification of a novel MCM3-associated protein that facilitates MCM3 nuclear localization”. J. Biol. Chem. 273 (35): 22177–80. DOI:10.1074/jbc.273.35.22177. PMID 9712829. 
  • Zhang JJ, Zhao Y, Chait BT, et al. (1999). „Ser727-dependent recruitment of MCM5 by Stat1alpha in IFN-gamma-induced transcriptional activation”. EMBO J. 17 (23): 6963–71. DOI:10.1093/emboj/17.23.6963. PMC 1171044. PMID 9843502. 
  • Yankulov K, Todorov I, Romanowski P, et al. (1999). „MCM Proteins Are Associated with RNA Polymerase II Holoenzyme”. Mol. Cell. Biol. 19 (9): 6154–63. PMC 84545. PMID 10454562. 
  • Fujita M, Yamada C, Goto H, et al. (1999). „Cell cycle regulation of human CDC6 protein. Intracellular localization, interaction with the human mcm complex, and CDC2 kinase-mediated hyperphosphorylation”. J. Biol. Chem. 274 (36): 25927–32. DOI:10.1074/jbc.274.36.25927. PMID 10464337. 
  • Kuwahara K, Yoshida M, Kondo E, et al. (2000). „A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of the germinal center and associated with MCM3, a protein essential for DNA replication”. Blood 95 (7): 2321–8. PMID 10733502. 
  • Hofmann Y, Becker J, Wright F, et al. (2000). „Genomic structure of the gene for the human P1 protein (MCM3) and its exclusion as a candidate for autosomal recessive polycystic kidney disease”. Eur. J. Hum. Genet. 8 (3): 163–6. DOI:10.1038/sj.ejhg.5200426. PMID 10780780. 
  • Abe E, Kuwahara K, Yoshida M, et al. (2000). „Structure, expression, and chromosomal localization of the human gene encoding a germinal center-associated nuclear protein (GANP) that associates with MCM3 involved in the initiation of DNA replication”. Gene 255 (2): 219–27. DOI:10.1016/S0378-1119(00)00336-X. PMID 11024281. 
  • p
  • r
  • u
Separacija
i inicijacija
Prokariotska
(inicijacija)
Eukariotska
(priprema u
G1 fazi)
Oba
Replikacija
Prokariotska
(elongacija)
Eukariotska
(sinteza u
S fazi)
Oba
Kretanje: Procesivnost  DNK ligaza
Terminacija
B bsyn: dnk (repl, cycl, reco, repr)  tscr (fact, tcrg, nucl, rnat, rept, ptts)  tltn (risu, pttl, nexn)  dnab, rnab/runp  stru (domn, 1°, 2°, 3°, 4°)