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Related Experiment Videos

Structure-function studies of the herpes simplex virus type 1 DNA polymerase.

M L Haffey1, J Novotny, R E Bruccoleri

  • 1Department of Virology, Squibb Institute for Medical Research, Princeton, New Jersey 08543-4000.

Journal of Virology
|October 1, 1990
PubMed
Summary

Herpes simplex virus type 1 DNA polymerase has distinct functional domains, similar to E. coli polymerase I. Mutagenesis and modeling studies identified key regions for DNA polymerization activity.

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Physiological research·2022

Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • Herpes simplex virus type 1 (HSV-1) DNA polymerase exhibits multiple catalytic activities: 5'-3'-exonuclease (RNase H), 3'-5'-exonuclease, and DNA polymerase.
  • Structural similarities are suggested between HSV-1 DNA polymerase and Escherichia coli polymerase I, implying domain-specific functions.

Purpose of the Study:

  • To define the structure and C-terminal limits of the catalytic domain responsible for DNA polymerization in HSV-1 DNA polymerase.
  • To investigate the functional roles of specific amino acid residues through in vitro mutagenesis and computer modeling.

Main Methods:

  • Deduced amino acid sequence analysis of HSV-1 DNA polymerase.
  • In vitro mutagenesis of the HSV-1 DNA polymerase gene.
  • Computer modeling based on the X-ray crystallographic structure of E. coli polymerase I.

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  • Expression of mutated HSV-1 DNA polymerase in Saccharomyces cerevisiae.

    • Main Results:

    • Sequence analysis predicts the major DNA polymerization domain resides between residues 690 and 1100.
    • A three-dimensional model of this region was generated, referencing E. coli polymerase I structure.
    • Deletion of C-terminal residues (1073-1144 and 1177-1235) and N-terminal residues (1-227) did not abolish HSV-1 DNA polymerase activity.

    Conclusions:

    • HSV-1 DNA polymerase activity is localized to a specific domain, with non-essential regions at the N and C termini.
    • The findings support a domain-based functional organization of the HSV-1 DNA polymerase, analogous to prokaryotic polymerases.