Abstract
The complete sequence of the reovirus (serotype 3) S1 gene was obtained by using cloned cDNA derived from the RNA segment. This gene is 1416 nucleotides in length and contains two open reading frames. The first reading frame has a coding capacity of 455 amino acids, sufficient to account for the known S1 product, protein ρ1 (42,000 MW). It possesses a signal peptide as well as three possible glycosylation sites. No homology could be detected when this gene sequence and the deduced amino acid sequence were compared to published sequences of the corresponding gene of a human rotavirus. The second reading frame (not in phase with the first) starts at the second ATG recently shown to be a functional initiation site. It has a coding capacity of 120 amino acids. Its outstanding feature is the highly basic amino-terminal region, a characteristic apparently shared by a number of DNA binding proteins. It is speculated that this protein, hitherto undetected, may play a role in mediating viral and/or host nucleic acid transcription.
Original language | English |
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Pages (from-to) | 8699-8710 |
Number of pages | 12 |
Journal | Nucleic Acids Research |
Volume | 12 |
Issue number | 22 |
DOIs | |
Publication status | Published - Nov 26 1984 |
Externally published | Yes |
Bibliographical note
Funding Information:ACKNOWLEDGEMENTS We thank Ralph Paul andTomonori Morinaga for stimulating discussions; David PotandMichael Yeung fortheir assistance with computer analysis of sequences; andShirley Eikerman for typing the manuscript. This work was supported by the Medical Research Council of Canada and by the Alberta Heritage Foundation for Medical Research (AHFMR). L.N. and D.C.W.M. arerecipients of AHFMR Studentships, andP.W.K.L. is anAHFMR Scholar.
ASJC Scopus Subject Areas
- Genetics