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Escherichia coli K-12 substr. MG1655 Protein: DNA polymerase III, core enzyme

Component of: DNA polymerase III, holoenzyme (extended summary available)

Subunit composition of DNA polymerase III, core enzyme = [DnaE][DnaQ][HolE]
         DNA polymerase III, α subunit = DnaE (extended summary available)
         DNA polymerase III, ε subunit = DnaQ (extended summary available)
         DNA polymerase III, θ subunit = HolE (extended summary available)

Summary:
The DNA polymerase III core enzyme contains one each of the alpha, epsilon and theta subunits and can carry out the basic polymerase and exonuclease activities of polymerase III [McHenry79].

Based on yeast two-hybrid data, both alpha and theta interact with epsilon, but not each other [Jonczyk98]. The interaction between epsilon and theta has been examined via lanthanide-labeling NMR [Pintacuda06]. In a cell-free translation system, theta is required for the generation of soluble epsilon. An NMR analysis of cell-free DNA core enzyme shows epsilon connects to alpha via a flexible linker region [Ozawa08].

Locations: cytosol

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol


Subunit of: DNA polymerase III, holoenzyme

Subunit composition of DNA polymerase III, holoenzyme = [(DnaE)(DnaQ)(HolE)]3[(DnaX)3(HolB)(HolA)][(DnaN)2]2[(DnaX)2][(HolC)(HolD)]4
         DNA polymerase III, core enzyme = (DnaE)(DnaQ)(HolE) (summary available)
                 DNA polymerase III, α subunit = DnaE (extended summary available)
                 DNA polymerase III, ε subunit = DnaQ (extended summary available)
                 DNA polymerase III, θ subunit = HolE (extended summary available)
         DNA polymerase III, preinitiation complex = (DnaX)3(HolB)(HolA) (extended summary available)
                 DNA polymerase III, τ subunit = DnaX
                 DNA polymerase III, δ prime subunit = HolB (summary available)
                 DNA polymerase III, δ subunit = HolA (summary available)
         DNA polymerase III, β subunit = (DnaN)2 (extended summary available)
         DNA polymerase III, τ subunit dimer = (DnaX)2 (extended summary available)
                 DNA polymerase III, τ subunit = DnaX
         DNA polymerase III, ψ-χ subunit = (HolC)(HolD) (extended summary available)
                 DNA polymerase III, χ subunit = HolC
                 DNA polymerase III, ψ subunit = HolD

Summary:
DNA polymerase III holoenzyme is the enzyme primarily responsible for replicative DNA synthesis in E. coli. It carries out primer-initiated 5' to 3' polymerization of DNA on a single-stranded DNA template, as well as 3' to 5' exonucleolytic editing of mispaired nucleotides.

Replicative DNA polymerization begins when the preinitiation complex binds single-stranded DNA near an RNA primer. The preinitiation complex then loads the beta processivity clamp onto the DNA at this site, after which three core polymerases, chaperoned into place by the tau subunit, bind to the processivity clamp, with one polymerase on the leading strand and two on the lagging. DNA is synthesized 5' to 3' from primers on both the leading and lagging strands, covalently attaching the newly synthesized DNA to the primer. Tau displaces beta in the presence of duplex DNA, dissociating the polymerase from the template when it reaches a temporary stop on the lagging strand or when synthesis is complete on either strand [Maki88, Maki88a, Onrust95, Maki88b, Nusslein76, ReyesLamothe10].

For more detailed discussion of the stages of polymerase binding and DNA synthesis, see the individual entries for DNA polymerase III, preinitiation complex, DNA polymerase III, β subunit, DNA polymerase III, τ subunit dimer, DNA polymerase III, core enzyme and their constituent parts.

DNA polymerase III binds a region about 30 nucleotides long upstream of the RNA primer, with the alpha subunit making contact 9 nucleotides upstream and the beta clamp making contact 22 nucleotides upstream [Reems95, Reems94]. The preinitiation complex binds an area larger than this prior to being displaced by the core polymerase [Reems94]. In the presence of DNA polymerase III, RNA primer length is limited to 10 nucleotides, a limitation that is independent of the epsilon-mediated 3' to 5' exonuclease activity [Zechner92].

During polymerization, DNA polymerase III pauses at sites of potential secondary structure [LaDuca83]. The holoenzyme can traverse distances as long as 400 base pairs of duplex DNA to reach the next available 3' end and restart synthesis [ODonnell85]. Such jumps within the same template take 2 to 5 seconds, whereas transfer to a new template takes 30 seconds [Burgers83].

DNA polymerase III is required for several kinds of DNA repair, including some forms of double-strand break repair, fixing hydrogen-peroxide-induced damage and methyl-directed mismatch repair [Motamedi99, Hagensee89, Cooper93]. Mutations that inhibit polymerase III stimulate repeat expansion and lead to lower levels of unsaturation in fatty acids [Morag99, Suzuki98].

UV mutagenesis and gap repair following UV damage to DNA both involve DNA polymerase III [CohenFix94, Tomer96]. The polymerase stalls at pyrimidine photodimers in vitro, but is capable of bypassing such lesions to continue synthesis [Shwartz87, Livneh86]. This bypass activity is stimulated by single-strand binding protein (SSB) but inhibited by the polymerase III beta subunit, which explains the relatively low rate of bypass in vivo [Shwartz87, Shavitt89].

Citations: [Cull95]

Credits:
Last-Curated ? 09-Jan-2006 by Shearer A , SRI International


Component enzyme of DNA polymerase III, core enzyme : DNA polymerase III, α subunit

Synonyms: SdgC, PolC, DnaE

Gene: dnaE Accession Numbers: EG10238 (EcoCyc), b0184, ECK0183

Locations: cytosol

Sequence Length: 1160 AAs

Molecular Weight: 129.9 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis Inferred from experiment [Maki85, UniProtGOA11a, GOA01, GOA01a]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0003887 - DNA-directed DNA polymerase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, GOA01a, Maki85]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Toste13, Jergic13, Kelman98, Kim96c, Rajagopala12, Stukenberg91, Ozawa08, Gao01, Butland05, Jonczyk98, Oishi06]
GO:0003676 - nucleic acid binding Inferred by computational analysis [GOA01a]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01a]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Maki85]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0044776 - DNA polymerase III, core complex Inferred from experiment [McHenry79]

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-9458N , EcoliWiki:b0184 , Mint:MINT-1224103 , ModBase:P10443 , PR:PRO_000022462 , Pride:P10443 , Protein Model Portal:P10443 , RefSeq:NP_414726 , SMR:P10443 , String:511145.b0184 , UniProt:P10443

Relationship Links: InterPro:IN-FAMILY:IPR003141 , InterPro:IN-FAMILY:IPR004013 , InterPro:IN-FAMILY:IPR004365 , InterPro:IN-FAMILY:IPR004805 , InterPro:IN-FAMILY:IPR011708 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR016195 , PDB:Structure:2HNH , PDB:Structure:2HQA , PDB:Structure:4GX8 , PDB:Structure:4GX9 , PDB:Structure:4JOM , Pfam:IN-FAMILY:PF01336 , Pfam:IN-FAMILY:PF02811 , Pfam:IN-FAMILY:PF07733 , Smart:IN-FAMILY:SM00481

Catalyzes:
a deoxyribonucleoside triphosphate + (deoxynucleotides)(n) = (deoxynucleotides)(n+1) + diphosphate

Summary:
The alpha subunit of DNA polymerase III catalyzes the polymerase activity of the holoenzyme complex [Maki85]. Replicative 5' to 3' polymerization of DNA requires dNTPs and template DNA with a bound RNA primer [Kornberg72, Hurwitz74]. The newly polymerized DNA is covalently attached to the RNA primer [Livingston75]. The presence of the epsilon subunit increases the polymerase activity of the alpha subunit two-fold [Maki87].

The alpha subunit is required for misincorporation and bypass during UV mutagenesis [Sharif90, Bridges90].

The middle portion of the alpha subunit (residues 542-991) is involved in binding to the polymerase III beta subunit. Deletion of the amino-terminal portion of alpha (residues 1-542) actually increases its affinity for beta [Kim96d]. The carboxy-terminus of alpha is required for binding to the polymerase III tau subunit [Kim96c]. The amino-terminal php domain of alpha is required for binding to the epsilon subunit [Wieczorek06].

Transcription of dnaE is induced by nalidixic acid, but not by mitomycin C, and induction does not require LexA [Van01].

Overproduction of alpha can compensate for an otherwise lethal deficiency in DNA polymerase I [Witkin92].

A crystal structure of the first 917 amino acids of DnaE has been determined to 2.3 Å resolution [Lamers06].

Citations: [Welch82]

Essentiality data for dnaE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Component enzyme of DNA polymerase III, core enzyme : DNA polymerase III, ε subunit

Synonyms: MutD, DnaQ

Gene: dnaQ Accession Numbers: EG10243 (EcoCyc), b0215, ECK0215

Locations: cytosol

Sequence Length: 243 AAs

Molecular Weight: 27.099 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0045004 - DNA replication proofreading Inferred from experiment [Echols83]
GO:0090305 - nucleic acid phosphodiester bond hydrolysis Inferred by computational analysis Inferred from experiment [Scheuermann84, UniProtGOA11a, GOA01a]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0004527 - exonuclease activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Scheuermann84]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Toste13, Jergic13, Hamdan02, Kelman98, Stukenberg91, Ozawa08, Butland05, Jonczyk98, Oishi06]
GO:0003676 - nucleic acid binding Inferred by computational analysis [GOA01a]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01a]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01, GOA01a]
GO:0004518 - nuclease activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0044776 - DNA polymerase III, core complex Inferred from experiment [McHenry79]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer DNA related DNA replication
information transfer protein related chaperoning, repair (refolding)

Unification Links: DIP:DIP-9462N , EcoliWiki:b0215 , Mint:MINT-1222832 , ModBase:P03007 , PR:PRO_000022467 , Protein Model Portal:P03007 , RefSeq:NP_414751 , SMR:P03007 , String:511145.b0215 , UniProt:P03007

Relationship Links: InterPro:IN-FAMILY:IPR006054 , InterPro:IN-FAMILY:IPR006055 , InterPro:IN-FAMILY:IPR006309 , InterPro:IN-FAMILY:IPR012337 , InterPro:IN-FAMILY:IPR013520 , PDB:Structure:1J53 , PDB:Structure:1J54 , PDB:Structure:1MGZ , PDB:Structure:2GUI , PDB:Structure:2IDO , PDB:Structure:2XY8 , PDB:Structure:4GX8 , PDB:Structure:4GX9 , Pfam:IN-FAMILY:PF00929 , Smart:IN-FAMILY:SM00479

Catalyzes:
DNAn + n H2O → n a nucleoside 5'-monophosphate

Summary:
The epsilon subunit of DNA polymerase III catalyzes the 3' to 5' proofreading exonuclease activity of the holoenzyme [Echols83, Livingston75a, Scheuermann84]. This activity is required to prevent spontaneous mutations and may play a role in preventing UV mutagenesis and lesion bypass synthesis as well [Woodgate87, Ciesla90, Pages05]. The epsilon subunit suppresses both misincorporation of dCMP and transversion mutations [Maki90, Wu90]. Episilon isrequired for speed and processivity of DNA polymerase III function [Studwell90].

In the presence of polymerase III alpha subunit, epsilon activity increases ten- to eighty-fold, and its affinity for the 3'-hydroxy terminus of DNA increases substantially [Maki87]. Single-stranded DNA binding protein inhibits epsilon activity during replication [Shwartz88].

The structure of epsilon complexed with a bacteriophage homolog of theta has been determined to 2.1 Å [Kirby06].

dnaQ is induced following exposure to various mutagenic and DNA-damaging substances, often in an SOS-response-dependent manner [Quinones90, Quinones89, Kaasch89, Quinones88].

In a dnaQ mutant, CAG and CTG trinucleotide repeats are destabilized and lose their orientation dependence. This effect appears to require SbcCD ATP-dependent dsDNA exonuclease [Zahra07].

Citations: [Scheuermann83, DiFrancesco84]

Essentiality data for dnaQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of DNA polymerase III, core enzyme: DNA polymerase III, θ subunit

Synonyms: HolE

Gene: holE Accession Numbers: EG11505 (EcoCyc), b1842, ECK1843

Locations: cytosol

Sequence Length: 76 AAs

Molecular Weight: 8.846 kD (from nucleotide sequence)

Molecular Weight: 10.0 kD (experimental) [McHenry79]

GO Terms:

Biological Process: GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11a]
GO:0006261 - DNA-dependent DNA replication Inferred by computational analysis [UniProtGOA11a, GOA01, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Hamdan02, Ozawa08, Jonczyk98, Butland05, Oishi06]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01a]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11a, GOA01, GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0044776 - DNA polymerase III, core complex Inferred from experiment [McHenry79]
GO:0005737 - cytoplasm

MultiFun Terms: information transfer DNA related DNA replication

Unification Links: DIP:DIP-39982N , EcoliWiki:b1842 , Mint:MINT-1223798 , ModBase:P0ABS8 , PR:PRO_000022920 , Pride:P0ABS8 , Protein Model Portal:P0ABS8 , RefSeq:NP_416356 , SMR:P0ABS8 , String:511145.b1842 , UniProt:P0ABS8

Relationship Links: InterPro:IN-FAMILY:IPR009052 , InterPro:IN-FAMILY:IPR011325 , PDB:Structure:1DU2 , PDB:Structure:2AE9 , PDB:Structure:2AXD , PDB:Structure:2XY8 , Pfam:IN-FAMILY:PF06440 , ProDom:IN-FAMILY:PD057609

Summary:
The theta subunit of DNA polymerase III (HolE) binds tightly to the epsilon subunit but not to the alpha subunit [StudwellVaughan93]. This binding appears to enhance interaction between alpha and epsilon as well as slightly stimulating epsilon proofreading activity [TaftBenz04, StudwellVaughan93]. Loss of theta yields no significant growth phenotype, and theta does not appear to be required for speed or processivity of DNA polymerase III holoenzyme [Slater94, Studwell90]. Theta may enhance the stability of epsilon [Conte12].

HolE may have a "moonlighting" function in the cell. Both YdgT and HolE appear to influence expression of tnaA by enhancing transcription termination at the leader DNA sequence [Dietrich13].

Based on an NMR characterization, the surface of theta is bipolar, with the positive and negative charges grouped at opposite ends of the protein [Keniry00]. It also appears to have exposed hydrophobic residues [Mueller05]. A solution structure of the theta in a complex with the N-terminal domain of epsilon has been solved [Keniry06].

A holE deletion strain appears to contain a lower amount of unassociated epsilon subunit [Conte12]. Microarray analysis of a holE mutant showed altered expression of a set of genes that overlapped significantly with genes whose expression was changed in a ydgT mutant [Dietrich13].

Citations: [Kim96e, Jonczyk98, Li99c, DeRose03, Gupta04, Ozawa08, Ozawa13]

Essentiality data for holE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

References

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Bridges90: Bridges BA, Bates H (1990). "Mutagenic DNA repair in Escherichia coli. XVIII. Involvement of DNA polymerase III alpha-subunit (DnaE protein) in mutagenesis after exposure to UV light." Mutagenesis 5(1);35-8. PMID: 2184309

Burgers83: Burgers PM, Kornberg A (1983). "The cycling of Escherichia coli DNA polymerase III holoenzyme in replication." J Biol Chem 258(12);7669-75. PMID: 6345527

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Ciesla90: Ciesla Z, Jonczyk P, Fijalkowska I (1990). "Effect of enhanced synthesis of the epsilon subunit of DNA polymerase III on spontaneous and UV-induced mutagenesis of the Escherichia coli glyU gene." Mol Gen Genet 221(2);251-5. PMID: 2196432

CohenFix94: Cohen-Fix O, Livneh Z (1994). "In vitro UV mutagenesis associated with nucleotide excision-repair gaps in Escherichia coli." J Biol Chem 269(7);4953-8. PMID: 8106470

Conte12: Conte E, Vincelli G, Schaaper RM, Bressanin D, Stefan A, Dal Piaz F, Hochkoeppler A (2012). "Stabilization of the Escherichia coli DNA polymerase III ε subunit by the θ subunit favors in vivo assembly of the Pol III catalytic core." Arch Biochem Biophys 523(2);135-43. PMID: 22546509

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Echols83: Echols H, Lu C, Burgers PM (1983). "Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme." Proc Natl Acad Sci U S A 80(8);2189-92. PMID: 6340117

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GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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Jergic13: Jergic S, Horan NP, Elshenawy MM, Mason CE, Urathamakul T, Ozawa K, Robinson A, Goudsmits JM, Wang Y, Pan X, Beck JL, van Oijen AM, Huber T, Hamdan SM, Dixon NE (2013). "A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode." EMBO J 32(9);1322-33. PMID: 23435564

Jonczyk98: Jonczyk P, Nowicka A, Fijalkowska IJ, Schaaper RM, Ciesla Z (1998). "In vivo protein interactions within the Escherichia coli DNA polymerase III core." J Bacteriol 180(6);1563-6. PMID: 9515927

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

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Kelman98: Kelman Z, Yuzhakov A, Andjelkovic J, O'Donnell M (1998). "Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly." EMBO J 17(8);2436-49. PMID: 9545254

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Kim96e: Kim DR, McHenry CS (1996). "In vivo assembly of overproduced DNA polymerase III. Overproduction, purification, and characterization of the alpha, alpha-epsilon, and alpha-epsilon-theta subunits." J Biol Chem 271(34);20681-9. PMID: 8702818

Kirby06: Kirby TW, Harvey S, DeRose EF, Chalov S, Chikova AK, Perrino FW, Schaaper RM, London RE, Pedersen LC (2006). "Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex." J Biol Chem 281(50):38466-71. PMID: 16973612

Kornberg72: Kornberg T, Gefter ML (1972). "Deoxyribonucleic acid synthesis in cell-free extracts. IV. Purification and catalytic properties of deoxyribonucleic acid polymerase III." J Biol Chem 247(17);5369-75. PMID: 4560196

LaDuca83: LaDuca RJ, Fay PJ, Chuang C, McHenry CS, Bambara RA (1983). "Site-specific pausing of deoxyribonucleic acid synthesis catalyzed by four forms of Escherichia coli DNA polymerase III." Biochemistry 22(22);5177-88. PMID: 6360204

Lamers06: Lamers MH, Georgescu RE, Lee SG, O'Donnell M, Kuriyan J (2006). "Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III." Cell 126(5);881-92. PMID: 16959568

Li99c: Li D, Allen DL, Harvey S, Perrino FW, Schaaper RM, London RE (1999). "A preliminary CD and NMR study of the Escherichia coli DNA polymerase III theta subunit." Proteins 36(1);111-6. PMID: 10373010

Livingston75: Livingston DM, Hinkle DC, Richardson CC (1975). "Deoxyribonucleic acid polymerase III of Escherichia coli. Purification and properties." J Biol Chem 250(2);461-9. PMID: 1089643

Livingston75a: Livingston DM, Richardson CC (1975). "Deoxyribonucleic acid polymerase III of Escherichia coli. Characterization of associated exonuclease activities." J Biol Chem 250(2);470-8. PMID: 163228

Livneh86: Livneh Z (1986). "Mechanism of replication of ultraviolet-irradiated single-stranded DNA by DNA polymerase III holoenzyme of Escherichia coli. Implications for SOS mutagenesis." J Biol Chem 261(20);9526-33. PMID: 2941423

Maki85: Maki H, Kornberg A (1985). "The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the alpha subunit, devoid of nuclease activities." J Biol Chem 260(24);12987-92. PMID: 2997151

Maki87: Maki H, Kornberg A (1987). "Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunits." Proc Natl Acad Sci U S A 84(13);4389-92. PMID: 3037519

Maki88: Maki S, Kornberg A (1988). "DNA polymerase III holoenzyme of Escherichia coli. III. Distinctive processive polymerases reconstituted from purified subunits." J Biol Chem 263(14);6561-9. PMID: 3283127

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