Abstract
The reovirus S1 gene has recently been shown potentially to encode two polypeptides (from two overlapping reading frames) having predicted molecular weights of 49,071 and 16,143. The larger polypeptide is reovirus protein σ 1, but synthesis of the smaller polypeptide has not been described to date. A truncated clone of the S1 gene in which the first ATG is deleted was expressed in an in vitro protein synthesis system to yield a ~13-kilodalton polypeptide, as determined from migration on sodium dodecyl sulfate-polyacrylamide gels. A polypeptide with a similar migration pattern on sodium dodecyl sulfate-polyacrylamide gels was present in reovirus-infected cells and absent from mock-infected cells. Comparative tryptic peptide analysis of the 13-kilodalton polypeptides produced in vivo and in vitro showed them to be identical. Thus, the s1 mRNA of reovirus type 3 is apparently bicistronic, and suggests that the ~13-kilodalton polypeptide be called σ s (standing for σ small).
Original language | English (US) |
---|---|
Pages (from-to) | 720-725 |
Number of pages | 6 |
Journal | Journal of virology |
Volume | 54 |
Issue number | 3 |
DOIs | |
State | Published - 1985 |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology