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DNA polymerase alpha

From Wikipedia, the free encyclopedia
Family of protein complexes
DNA-directed DNA polymerase
Identifiers
EC no.2.7.7.7
CAS no.9012-90-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDBPDBePDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Shared primase-binding peptide in archaealPolD and eukaryotic Polα[1]

DNA polymerase alpha, also known asPol α, is anenzyme complex found ineukaryotes that is involved in initiation ofDNA replication. The DNA polymerase alpha complex consists of 4 subunits:POLA1,POLA2,PRIM1, andPRIM2.[2]

Pol α has limitedprocessivity and lacks 3′exonuclease activity for proofreading errors. Thus it is not well suited to efficiently and accurately copy long templates (unlike PolDelta andEpsilon). Instead, it plays a more limited role in replication. Pol α is responsible for the initiation of DNA replication at origins of replication (on both the leading and lagging strands) and during synthesis ofOkazaki fragments on the lagging strand. The Pol α complex (pol α-DNA primase complex) consists of four subunits: the catalytic subunit POLA1, the regulatory subunitPOLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Once primase has created the RNA primer, Pol α starts replication elongating the primer with ~20 nucleotides.[2]

Structure

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DNA polymerase alpha, likeDNA primase, contains iron-sulfur clusters, that are critical inelectron transport that uses DNA itself to transfer electrons at very high speeds; this process is involved in detecting DNA damage, and may also be involved in a feedback between the primase complex and the DNA polymerase alpha.[3]

References

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  1. ^Madru, Clément; Henneke, Ghislaine; Raia, Pierre; Hugonneau-Beaufet, Inès; Pehau-Arnaudet, Gérard; England, Patrick; Lindahl, Erik; Delarue, Marc; Carroni, Marta; Sauguet, Ludovic (December 2020)."Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA".Nature Communications.11 (1): 1591.Bibcode:2020NatCo..11.1591M.doi:10.1038/s41467-020-15392-9.PMC 7101311.PMID 32221299.
  2. ^abLehman IR, Kaguni LS (March 1989)."DNA polymerase alpha"(PDF).J. Biol. Chem.264 (8):4265–8.doi:10.1016/S0021-9258(18)83733-4.PMID 2647732.
  3. ^"Electrons use DNA like a wire for signaling DNA replication".

External links

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Initiation
Prokaryotic
(initiation)
Eukaryotic
(preparation in
G1 phase
)
Both
Replication
Prokaryotic
(elongation)
Eukaryotic
(synthesis in
S phase
)
Both
Termination
Transferases:phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1:OH acceptor
2.7.2:COOH acceptor
2.7.3:N acceptor
2.7.4:PO4 acceptor
2.7.6:diphosphotransferase
(P2O7)
2.7.7:nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5'exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13:protein kinase
(PO4; protein acceptor)
2.7.10:protein-tyrosine
2.7.11:protein-serine/threonine
2.7.12: protein-dual-specificity
2.7.13: protein-histidine
Activity
Regulation
Classification
Kinetics
Types
Portal:

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.


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