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Archaeal DNA Polymerases: Enzymatic Abilities, Coordination, and Unique Properties

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Nucleic Acid Polymerases

Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC,volume 30))

Abstract

DNA polymerases from archaea coordinate both replication and repair activities under extreme conditions. Traditional DNA polymerase families B and Y are represented, but an entire phylum of archaea contains members from the unique D-family. These model archaeal polymerases from each family have be exploited for a variety of biotechnology applications but have also provided great insight into kinetic mechanisms, structural properties, conformational changes, and protein interactions with DNA polymerases from other domains. Interestingly, individual polymerase members have revealed some unique features including template uracil recognition, more open active sites, novel motifs, and direct polymerase interactions that modulate replication and repair in these simpler organisms. How multiple polymerases coordinate synthesis on the leading and lagging strands and replication or repair duties is an ongoing fundamental question in archaea. Nevertheless, their intrinsic enzymatic properties are fascinating and continue to shape and influence research avenues for all DNA polymerases. The ability to regulate robust and accurate DNA synthesis through specific and loosely associate oligomeric states and protein interactions maintains a high degree of genomic stability in spite of harsh environmental conditions.

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Abbreviations

BER:

Base excision repair

NER:

Nucleotide excision repair

NTP:

Nucleotide triphosphate

Pab :

Pyrococcus abyssi

PCNA:

Proliferating cellular nuclear antigen

Pfu :

Pyrococcus furiosus

Pho :

Pyrococcus horikoshii

Pol:

Polymerase

PPi :

Pyrophosphate

RFC:

Replication factor C

Sac :

Sulfolobus acidocaldarius

Sso :

Sulfolobus solfataricus

Tgo :

Thermococcus gorgonarius

UV:

Ultraviolet

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Authors and Affiliations

  1. Department of Chemistry, University of Pittsburgh, 219 Parkman Ave, 801 Chevron, Pittsburgh, PA, 15260, USA

    Michael A. Trakselis & Robert J. Bauer

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  1. Michael A. Trakselis
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  2. Robert J. Bauer
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Correspondence to Michael A. Trakselis .

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  1. Dept. of Biochem. and Mol. Biology, The Pennsylvania State University, University Park, Pennsylvania, USA

    Katsuhiko S. Murakami

  2. Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania, USA

    Michael A. Trakselis

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Trakselis, M.A., Bauer, R.J. (2014). Archaeal DNA Polymerases: Enzymatic Abilities, Coordination, and Unique Properties. In: Murakami, K., Trakselis, M. (eds) Nucleic Acid Polymerases. Nucleic Acids and Molecular Biology, vol 30. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-39796-7_6

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