Polyoma viruses with mutations at endonuclease HindII site 1: alterations at the COOH terminus of VP1
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Abstract:
Four mutants of polyoma virus lacking endonuclease HindII site 1 were isolated and characterized with respect to the VP1 coding sequence. Three of these mutants had deletions that removed 0.2 to 0.3% of the genome. All three deletion mutants encoded VP1 proteins that were smaller than wild type and that lacked one or more tryptic peptides normally found in the wild-type VP1 protein. Our results suggest the HindII site 1 is at, or very near, the carboxy terminal end of the coding sequence for VP1. A model for the peptide organization in that region is presented.
Insights
Researchers studied polyoma virus mutants lacking a specific DNA site. Deletions in these mutants altered the VP1 protein, suggesting the site is crucial for VP1
Area of Science:
- Molecular biology
- Virology
- Genetics
Background:
- Polyoma virus is a model organism for studying viral gene expression.
- The VP1 protein is the major capsid protein of polyoma virus.
- Endonuclease HindII is an enzyme used for DNA manipulation.
Purpose of the Study:
- To investigate the function of the HindII site 1 in polyoma virus.
- To characterize polyoma virus mutants with deletions at the HindII site 1.
- To determine the location of the HindII site 1 relative to the VP1 coding sequence.
Main Methods:
- Isolation and characterization of polyoma virus mutants.
- DNA sequencing to identify deletions.
- Tryptic peptide analysis of VP1 proteins.
Main Results:
- Four polyoma virus mutants lacking HindII site 1 were generated.
- Three mutants had small deletions (0.2-0.3% of the genome).
- Deletion mutants produced smaller VP1 proteins lacking specific tryptic peptides.
Conclusions:
- The HindII site 1 is located at or near the C-terminal end of the VP1 coding sequence.
- This site is important for the integrity of the VP1 protein.
- A model for VP1 peptide organization was proposed.