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DNA Polymerase III Structure

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Molecular Life Sciences

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Synopsis

By itself, the polymerase catalytic subunit of the DNA polymerase III holoenzyme (Pol III HE), α, exhibits no special properties that hint of the Pol III HE’s high catalytic efficiency, accuracy, and enormous processivity. These properties are gained by association with other proteins through a series of distinct protein interaction domains. A PHP domain at the N-terminus of Pol III α binds the proofreading subunit, ε. A typical Mg++-dependent polymerase catalytic domain has a fold similar to the DNA polymerase β (Pol X family). Adjacent to the polymerase domain is the β-binding domain. Interaction of this domain with the β2 sliding clamp processivity factor, together with an ε−β2interaction, provides the primary determinants of the enzyme’s processivity. The C-terminus contains two domains, one an OB fold that may bind single-stranded DNA and a τ-binding domain that binds the τ-subunit of the DnaX complex. X-ray crystal structures of Pol III α in the apoenzyme form, bound...

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Authors and Affiliations

  1. Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO, USA

    Charles McHenry

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  1. Charles McHenry
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Correspondence to Charles McHenry .

Editor information

Editors and Affiliations

  1. Department of Chemistry, Texas A&M University, College Station, Texas, USA

    Robert D. Wells

  2. Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, Pennsylvania, USA

    Judith S. Bond

  3. Department of Chemistry Department of Molecular and Cell Biology, University of California The california institute for Quanti, Berkeley, California, USA

    Judith Klinman

  4. Department of Biochemistry, The University of Texas Health Science C, San Antonio, Texas, USA

    Bettie Sue Siler Masters

  5. Dept of Chemistry, University of Richmond, Richmond, Virginia, USA

    Ellis Bell

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McHenry, C. (2014). DNA Polymerase III Structure. In: Wells, R., Bond, J., Klinman, J., Masters, B., Bell, E. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6436-5_131-1

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  • DOI: https://doi.org/10.1007/978-1-4614-6436-5_131-1

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  • Online ISBN: 978-1-4614-6436-5

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