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Escherichia coli K-12 substr. MG1655 Enzyme: DNA polymerase III, ε subunit



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

Synonyms: mutD

Regulation Summary Diagram: ?

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

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]

Gene Citations: [Nomura85]

Locations: cytosol

Map Position: [236,067 -> 236,798] (5.09 centisomes)
Length: 732 bp / 243 aa

Molecular Weight of Polypeptide: 27.099 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000722 , CGSC:840 , DIP:DIP-9462N , EchoBASE:EB0239 , EcoGene:EG10243 , EcoliWiki:b0215 , Mint:MINT-1222832 , ModBase:P03007 , OU-Microarray:b0215 , PortEco:dnaQ , PR:PRO_000022467 , Protein Model Portal:P03007 , RefSeq:NP_414751 , RegulonDB:EG10243 , 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

Gene-Reaction Schematic: ?

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, UniProtGOA11, GOA01]
GO:0006260 - DNA replication Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0004527 - exonuclease activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, 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 [GOA01]
GO:0003677 - DNA binding Inferred by computational analysis [GOA01]
GO:0003887 - DNA-directed DNA polymerase activity Inferred by computational analysis [UniProtGOA11, GOA01a, GOA01]
GO:0004518 - nuclease activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
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)

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 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Enzymatic reaction of: 3' to 5' proofreading exonuclease (DNA polymerase III, ε subunit)

EC Number: 3.1.11.-

DNAn + n H2O <=> n a nucleoside 5'-monophosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Subunit of: DNA polymerase III, core enzyme

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)

Component of: DNA polymerase III, holoenzyme (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

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


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 12
[UniProt10]
UniProt: Divalent metal cation 1; catalytic;
Metal-Binding-Site 14
[UniProt10]
UniProt: Divalent metal cation 1; catalytic;
Amino-Acid-Sites-That-Bind 61
[UniProt10]
UniProt: Substrate;
Amino-Acid-Sites-That-Bind 66
[UniProt10]
UniProt: Substrate;
Active-Site 162
[UniProt10]
UniProt: Proton acceptor;
Metal-Binding-Site 167
[UniProt10]
UniProt: Divalent metal cation 1; catalytic;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0215 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10243; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

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

Cooper93: Cooper DL, Lahue RS, Modrich P (1993). "Methyl-directed mismatch repair is bidirectional." J Biol Chem 268(16);11823-9. PMID: 8389365

Cull95: Cull MG, McHenry CS (1995). "Purification of Escherichia coli DNA polymerase III holoenzyme." Methods Enzymol 262;22-35. PMID: 8594350

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

DiFrancesco84: DiFrancesco R, Bhatnagar SK, Brown A, Bessman MJ (1984). "The interaction of DNA polymerase III and the product of the Escherichia coli mutator gene, mutD." J Biol Chem 259(9);5567-73. PMID: 6325441

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Hagensee89: Hagensee ME, Moses RE (1989). "Multiple pathways for repair of hydrogen peroxide-induced DNA damage in Escherichia coli." J Bacteriol 171(2);991-5. PMID: 2644241

Hamdan02: Hamdan S, Bulloch EM, Thompson PR, Beck JL, Yang JY, Crowther JA, Lilley PE, Carr PD, Ollis DL, Brown SE, Dixon NE (2002). "Hydrolysis of the 5'-p-nitrophenyl ester of TMP by the proofreading exonuclease (epsilon) subunit of Escherichia coli DNA polymerase III." Biochemistry 41(16);5266-75. PMID: 11955076

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

Kaasch89: Kaasch M, Kaasch J, Quinones A (1989). "Expression of the dnaN and dnaQ genes of Escherichia coli is inducible by mitomycin C." Mol Gen Genet 219(1-2);187-92. PMID: 2515428

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

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

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

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

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

Maki88a: Maki S, Kornberg A (1988). "DNA polymerase III holoenzyme of Escherichia coli. II. A novel complex including the gamma subunit essential for processive synthesis." J Biol Chem 263(14);6555-60. PMID: 3283126

Maki88b: Maki H, Maki S, Kornberg A (1988). "DNA Polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites." J Biol Chem 263(14);6570-8. PMID: 3283128

Maki90: Maki H, Akiyama M, Horiuchi T, Sekiguchi M (1990). "Molecular mechanisms of replicational fidelity in Escherichia coli." Basic Life Sci 52;299-308. PMID: 2158294

McHenry79: McHenry CS, Crow W (1979). "DNA polymerase III of Escherichia coli. Purification and identification of subunits." J Biol Chem 254(5);1748-53. PMID: 368075

Morag99: Morag AS, Saveson CJ, Lovett ST (1999). "Expansion of DNA repeats in Escherichia coli: effects of recombination and replication functions." J Mol Biol 289(1);21-7. PMID: 10339402

Motamedi99: Motamedi MR, Szigety SK, Rosenberg SM (1999). "Double-strand-break repair recombination in Escherichia coli: physical evidence for a DNA replication mechanism in vivo." Genes Dev 13(21);2889-903. PMID: 10557215

Nomura85: Nomura T, Aiba H, Ishihama A (1985). "Transcriptional organization of the convergent overlapping dnaQ-rnh genes of Escherichia coli." J Biol Chem 1985;260(11);7122-5. PMID: 2987244

Nusslein76: Nusslein V, Henke S, Johnston LH (1976). "Replication of E. coli duplex DNA in vitro. The separation of the DNA containing fractions of a lysate from the soluble enzymes and their complementation properties." Mol Gen Genet 145(2);183-90. PMID: 778584

ODonnell85: O'Donnell ME, Kornberg A (1985). "Dynamics of DNA polymerase III holoenzyme of Escherichia coli in replication of a multiprimed template." J Biol Chem 260(23);12875-83. PMID: 2413035

Oishi06: Oishi Y, Yunomura S, Kawahashi Y, Doi N, Takashima H, Baba T, Mori H, Yanagawa H (2006). "Escherichia coli proteome chips for detecting protein-protein interactions." Proteomics 6(24);6433-6. PMID: 17109382

Onrust95: Onrust R, Finkelstein J, Turner J, Naktinis V, O'Donnell M (1995). "Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. III. Interface between two polymerases and the clamp loader." J Biol Chem 270(22);13366-77. PMID: 7768938

Ozawa08: Ozawa K, Jergic S, Park AY, Dixon NE, Otting G (2008). "The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker." Nucleic Acids Res 36(15);5074-82. PMID: 18663010

Pages05: Pages V, Janel-Bintz R, Fuchs RP (2005). "Pol III proofreading activity prevents lesion bypass as evidenced by its molecular signature within E.coli cells." J Mol Biol 352(3);501-9. PMID: 16111701

Pintacuda06: Pintacuda G, Park AY, Keniry MA, Dixon NE, Otting G (2006). "Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes." J Am Chem Soc 128(11);3696-702. PMID: 16536542

Quinones88: Quinones A, Piechocki R, Messer W (1988). "Expression of the Escherichia coli dnaQ (mutD) gene is inducible." Mol Gen Genet 211(1);106-12. PMID: 2830459

Quinones89: Quinones A, Kaasch J, Kaasch M, Messer W (1989). "Induction of dnaN and dnaQ gene expression in Escherichia coli by alkylation damage to DNA." EMBO J 8(2);587-93. PMID: 2656258

Quinones90: Quinones A (1990). "Regulation of the dnaQ gene of Escherichia coli in mutants expressing the SOS regulon constitutively." J Basic Microbiol 30(5);353-62. PMID: 2242163

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reems94: Reems JA, McHenry CS (1994). "Escherichia coli DNA polymerase III holoenzyme footprints three helical turns of its primer." J Biol Chem 269(52);33091-6. PMID: 7806536

Reems95: Reems JA, Wood S, McHenry CS (1995). "Escherichia coli DNA polymerase III holoenzyme subunits alpha, beta, and gamma directly contact the primer-template." J Biol Chem 270(10);5606-13. PMID: 7890680

ReyesLamothe10: Reyes-Lamothe R, Sherratt DJ, Leake MC (2010). "Stoichiometry and architecture of active DNA replication machinery in Escherichia coli." Science 328(5977);498-501. PMID: 20413500

Scheuermann83: Scheuermann R, Tam S, Burgers PM, Lu C, Echols H (1983). "Identification of the epsilon-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: a fidelity subunit for DNA replication." Proc Natl Acad Sci U S A 80(23);7085-9. PMID: 6359162

Scheuermann84: Scheuermann RH, Echols H (1984). "A separate editing exonuclease for DNA replication: the epsilon subunit of Escherichia coli DNA polymerase III holoenzyme." Proc Natl Acad Sci U S A 81(24);7747-51. PMID: 6393125

Shavitt89: Shavitt O, Livneh Z (1989). "The beta subunit modulates bypass and termination at UV lesions during in vitro replication with DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 264(19);11275-81. PMID: 2661556

Shwartz87: Shwartz H, Livneh Z (1987). "Dynamics of termination during in vitro replication of ultraviolet-irradiated DNA with DNA polymerase III holoenzyme of Escherichia coli." J Biol Chem 262(22);10518-23. PMID: 2956258

Shwartz88: Shwartz H, Shavitt O, Livneh Z (1988). "The role of exonucleolytic processing and polymerase-DNA association in bypass of lesions during replication in vitro. Significance for SOS-targeted mutagenesis." J Biol Chem 263(34);18277-85. PMID: 3056941

Studwell90: Studwell PS, O'Donnell M (1990). "Processive replication is contingent on the exonuclease subunit of DNA polymerase III holoenzyme." J Biol Chem 265(2);1171-8. PMID: 2153103

Stukenberg91: Stukenberg PT, Studwell-Vaughan PS, O'Donnell M (1991). "Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme." J Biol Chem 266(17);11328-34. PMID: 2040637

Suzuki98: Suzuki E, Kondo T, Makise M, Mima S, Sakamoto K, Tsuchiya T, Mizushima T (1998). "Alteration in levels of unsaturated fatty acids in mutants of Escherichia coli defective in DNA replication." Biol Pharm Bull 21(7);657-61. PMID: 9703244

Tomer96: Tomer G, Cohen-Fix O, O'Donnell M, Goodman M, Livneh Z (1996). "Reconstitution of repair-gap UV mutagenesis with purified proteins from Escherichia coli: a role for DNA polymerases III and II." Proc Natl Acad Sci U S A 93(4);1376-80. PMID: 8643639

Toste13: Toste Rego A, Holding AN, Kent H, Lamers MH (2013). "Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair." EMBO J 32(9);1334-43. PMID: 23549287

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Woodgate87: Woodgate R, Bridges BA, Herrera G, Blanco M (1987). "Mutagenic DNA repair in Escherichia coli. XIII. Proofreading exonuclease of DNA polymerase III holoenzyme is not operational during UV mutagenesis." Mutat Res 183(1);31-7. PMID: 3025722

Wu90: Wu TH, Clarke CH, Marinus MG (1990). "Specificity of Escherichia coli mutD and mutL mutator strains." Gene 87(1);1-5. PMID: 2185133

Zahra07: Zahra R, Blackwood JK, Sales J, Leach DR (2007). "Proofreading and Secondary Structure Processing Determine the Orientation Dependence of CAG{middle dot}CTG Trinucleotide Repeat Instability in Escherichia coli." Genetics 176(1):27-41. PMID: 17339223

Zechner92: Zechner EL, Wu CA, Marians KJ (1992). "Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. III. A polymerase-primase interaction governs primer size." J Biol Chem 267(6);4054-63. PMID: 1531480


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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