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Determination of the origin-specific DNA-binding domain of polyomavirus large T antigen

N A Sunstrom1, N H Acheson, J A Hassell

  • 1Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada.

Journal of Virology
|December 1, 1991
PubMed

Insights

Researchers mapped the polyomavirus large T antigen DNA-binding domain. This crucial region, essential for viral DNA replication, spans amino acids 282 to 398.

Area of Science:

  • Molecular Biology
  • Virology
  • Protein Biochemistry

Background:

  • Polyomavirus large T antigen is essential for viral DNA replication.
  • Understanding its DNA-binding domain is key to elucidating viral mechanisms.

Purpose of the Study:

  • To precisely map the DNA-binding domain of the polyomavirus large T antigen.
  • To identify the specific amino acid residues involved in origin DNA recognition.

Main Methods:

  • Construction of plasmids encoding carboxy- and amino-terminal deletion mutants of large T antigen.
  • Expression of mutant proteins in Cos-1 cells and analysis of origin-specific DNA binding.
  • Evaluation of point mutants and internal deletions reported by other studies.

Main Results:

  • The C-terminal boundary of the DNA-binding domain was identified at or near Glu-398.
  • Fusion proteins lacking the first 200 N-terminal amino acids retained specific DNA binding.
  • The N-terminal boundary was localized between amino acids 282 and 286, based on previous studies.

Conclusions:

  • The DNA-binding domain of polyomavirus large T antigen is located within the 116-amino-acid region between residues 282 and 398.
  • This defined region is critical for the specific recognition and binding of viral origin DNA.

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