POLE (gene)

VALUE_ERROR (nil)

Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

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Ensembl| |

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UniProt| |

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RefSeq (mRNA)| |

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RefSeq (protein)| |

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Location (UCSC)| n/a| n/a
PubMed search| n/a| n/a
Wikidata
| View/Edit Human|

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DNA polymerase epsilon catalytic subunit is an enzyme that in humans is encoded by the POLE gene.[1][2] It is the central catalytic subunit of DNA polymerase epsilon.

## Contents

* 1 Clinical significance
* 2 Interactions
* 3 References
* 4 Further reading

## Clinical significance

[edit | edit source]

POLE, along with POLD1, has recently been associated with multiple adenoma.[3]

## Interactions

[edit | edit source]

POLE has been shown to interact with RAD17.[4]

## References

[edit | edit source]

1. ↑ Szpirer J, Pedeutour F, Kesti T, Riviere M, Syväoja JE, Turc-Carel C, Szpirer C (Aug 1994). "Localization of the gene for DNA polymerase epsilon (POLE) to human chromosome 12q24.3 and rat chromosome 12 by somatic cell hybrid panels and fluorescence in situ hybridization". Genomics. 20 (2): 223–6. doi:10.1006/geno.1994.1156. PMID 8020968.
2. ↑ "Entrez Gene: POLE polymerase (DNA directed), epsilon".
3. ↑ Palles C, Cazier JB, Howarth KM, Domingo E, Jones AM, Broderick P, Kemp Z, Spain SL, Guarino E, Guarino Almeida E, Salguero I, Sherborne A, Chubb D, Carvajal-Carmona LG, Ma Y, Kaur K, Dobbins S, Barclay E, Gorman M, Martin L, Kovac MB, Humphray S, Lucassen A, Holmes CC, Bentley D, Donnelly P, Taylor J, Petridis C, Roylance R, Sawyer EJ, Kerr DJ, Clark S, Grimes J, Kearsey SE, Thomas HJ, McVean G, Houlston RS, Tomlinson I (2013). "Germline mutations affecting the proofreading domains of POLE and POLD1 predispose to colorectal adenomas and carcinomas". Nat. Genet. 45 (2): 136–44. doi:10.1038/ng.2503. PMC 3785128. PMID 23263490.
4. ↑ Post SM, Tomkinson AE, Lee EY (Oct 2003). "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon". Nucleic Acids Res. England. 31 (19): 5568–75. doi:10.1093/nar/gkg765. PMC 206465. PMID 14500819.

## Further reading

[edit | edit source]

* Popanda O, Thielmann HW (1992). "The function of DNA polymerases in DNA repair synthesis of ultraviolet-irradiated human fibroblasts". Biochim. Biophys. Acta. 1129 (2): 155–60. doi:10.1016/0167-4781(92)90480-N. PMID 1730053.
* Kesti T, Frantti H, Syväoja JE (1993). "Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon". J. Biol. Chem. 268 (14): 10238–45. PMID 8486689.
* Mozzherin DJ, Fisher PA (1996). "Human DNA polymerase epsilon: enzymologic mechanism and gap-filling synthesis". Biochemistry. 35 (11): 3572–7. doi:10.1021/bi952142p. PMID 8639508.
* Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Mol. Cell. Biol. 17 (4): 1817–23. PMC 232028. PMID 9121429.
* Coll JM, Hickey RJ, Cronkey EA, Jiang HY, Schnaper L, Lee MY, Uitto L, Syvaoja JE, Malkas LH (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.
* Huang D, Pospiech H, Kesti T, Syväoja JE (1999). "Structural organization and splice variants of the POLE1 gene encoding the catalytic subunit of human DNA polymerase epsilon". Biochem. J. 339 (3): 657–65. doi:10.1042/0264-6021:3390657. PMC 1220202. PMID 10215605.
* Araújo SJ, Tirode F, Coin F, Pospiech H, Syväoja JE, Stucki M, Hübscher U, Egly JM, Wood RD (2000). "Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK". Genes Dev. 14 (3): 349–59. PMC 316364. PMID 10673506.
* Li Y, Pursell ZF, Linn S (2000). "Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon". J. Biol. Chem. 275 (30): 23247–52. doi:10.1074/jbc.M002548200. PMID 10801849.
* Mäkiniemi M, Hillukkala T, Tuusa J, Reini K, Vaara M, Huang D, Pospiech H, Majuri I, Westerling T, Mäkelä TP, Syväoja JE (2001). "BRCT domain-containing protein TopBP1 functions in DNA replication and damage response". J. Biol. Chem. 276 (32): 30399–406. doi:10.1074/jbc.M102245200. PMID 11395493.
* Fuss J, Linn S (2002). "Human DNA polymerase epsilon colocalizes with proliferating cell nuclear antigen and DNA replication late, but not early, in S phase". J. Biol. Chem. 277 (10): 8658–66. doi:10.1074/jbc.M110615200. PMID 11741962.
* Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". J. Biol. Chem. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
* Post SM, Tomkinson AE, Lee EY (2003). "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon". Nucleic Acids Res. 31 (19): 5568–75. doi:10.1093/nar/gkg765. PMC 206465. PMID 14500819.
* Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
* Clark AG, Glanowski S, Nielsen R, Thomas PD, Kejariwal A, Todd MA, Tanenbaum DM, Civello D, Lu F, Murphy B, Ferriera S, Wang G, Zheng X, White TJ, Sninsky JJ, Adams MD, Cargill M (2003). "Inferring nonneutral evolution from human-chimp-mouse orthologous gene trios". Science. 302 (5652): 1960–3. doi:10.1126/science.1088821. PMID 14671302.
* Rytkönen AK, Vaara M, Nethanel T, Kaufmann G, Sormunen R, Läärä E, Nasheuer HP, Rahmeh A, Lee MY, Syväoja JE, Pospiech H (2006). "Distinctive activities of DNA polymerases during human DNA replication". FEBS J. 273 (13): 2984–3001. doi:10.1111/j.1742-4658.2006.05310.x. PMID 16762037.
* Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

* v
* t
* e

DNA replication (comparing Prokaryotic to Eukaryotic)

Initiation|

| Prokaryotic
(initiation)|

* Pre-replication complex

* dnaC
* 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 fragments
* 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:
* alpha
* POLA1
* POLA2
* PRIM1
* PRIM2
* delta
* POLD1
* POLD2
* POLD3
* POLD4
* epsilon
* POLE
* POLE2
* POLE3
* POLE4

* DNA clamp
* PCNA

* Control of chromosome duplication

Both|

* Movement: Processivity
* DNA ligase

Termination|

* Telomere: Telomerase
* TERT
* TERC
* DKC1

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