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    dnaE DNA polymerase III subunit alpha [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944877, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    results support a model in which the pol and exo activities of pol III core are effectively independent, and in which recognition of the 3' end of the primer by either alpha or epsilon is governed by the primer stability.

    Single-molecule mechanochemical characterization of E. coli pol III core catalytic activity.
    Naufer MN, Murison DA, Rouzina I, Beuning PJ, Williams MC., Free PMC Article

    08/12/2017
    Mutation in PHP domain of Pol III alpha ablated interaction with the proofreading subunit.

    DNA Polymerase α Subunit Residues and Interactions Required for Efficient Initiation Complex Formation Identified by a Genetic Selection.
    Lindow JC, Dohrmann PR, McHenry CS., Free PMC Article

    10/31/2015
    Data show that the tau (tau), alpha (alpha), epsilon (epsilon), and theta (theta;) subunits of DNA Polymerase III can be assembled in vivo, yielding the trimeric tau3alpha3epsilon3theta;3 complex.

    Simultaneous ternary extension of DNA catalyzed by a trimeric replicase assembled in vivo.
    Montón Silva A, Lapenta F, Stefan A, Dal Piaz F, Ceccarelli A, Perrone A, Hochkoeppler A.

    08/15/2015
    The results suggest that competition between UmuD and ssDNA for DNA polymerase III alpha binding is a new mechanism for polymerase exchange.

    Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.
    Chaurasiya KR, Ruslie C, Silva MC, Voortman L, Nevin P, Lone S, Beuning PJ, Williams MC., Free PMC Article

    01/4/2014
    The PHP domain is a major structural element in Pol III and its integrity modulates both the stability and activity of the polymerase.

    A structural role for the PHP domain in E. coli DNA polymerase III.
    Barros T, Guenther J, Kelch B, Anaya J, Prabhakar A, O'Donnell M, Kuriyan J, Lamers MH., Free PMC Article

    12/21/2013
    Authors demonstrate for the first time that the major DNA polymerases (Pol I and Pol III) and DNA ligase are directly involved with oligo recombination.

    Bacterial DNA polymerases participate in oligonucleotide recombination.
    Li XT, Thomason LC, Sawitzke JA, Costantino N, Court DL., Free PMC Article

    12/21/2013
    Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB

    [Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB].
    Mel'kina OE, Gorianin II, Manukhov IV, Zavil'gel'skiĭ GB.

    08/31/2013
    A structural model of the alphaepsilontheta;:beta2 replicase complex reveals a compact, but still flexible, structure of the complex.

    Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain.
    Ozawa K, Horan NP, Robinson A, Yagi H, Hill FR, Jergic S, Xu ZQ, Loscha KV, Li N, Tehei M, Oakley AJ, Otting G, Huber T, Dixon NE., Free PMC Article

    07/27/2013
    Authors report that DNA pol III incorporates 8-oxo-dGTP approximately 20 times more efficiently opposite template A compared with template C.

    Escherichia coli DNA polymerase III is responsible for the high level of spontaneous mutations in mutT strains.
    Yamada M, Shimizu M, Katafuchi A, Grúz P, Fujii S, Usui Y, Fuchs RP, Nohmi T., Free PMC Article

    06/1/2013
    Authors propose that the interaction between DNA polymerase III alpha and UmuD contributes to the transition between replicative and translesion synthesis polymerases by removing DNA polymerase III alpha from the beta clamp.

    Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.
    Silva MC, Nevin P, Ronayne EA, Beuning PJ., Free PMC Article

    10/6/2012
    Data indicate that tripolymerase replisomes are much more processive than dipolymerase replisomes.

    Single-molecule studies reveal the function of a third polymerase in the replisome.
    Georgescu RE, Kurth I, O'Donnell ME., Free PMC Article

    03/10/2012
    Data shows that the proofreading domain of epsilon subunit is connected to alpha via a flexible linker peptide comprising over 20 residues.

    The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.
    Ozawa K, Jergic S, Park AY, Dixon NE, Otting G., Free PMC Article

    01/21/2010
    Here we show that, in contrast to distributive DNA synthesis exhibited by wild-type alpha subunit, the dnaE173 mutant form of alpha subunit catalyzes highly processive DNA chain elongation without the aid of the beta-clamp

    The dnaE173 mutator mutation confers on the alpha subunit of Escherichia coli DNA polymerase III a capacity for highly processive DNA synthesis and stable binding to primer/template DNA.
    Yanagihara F, Yoshida S, Sugaya Y, Maki H.

    01/21/2010
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