| Autor: |
Kiefer MC; Department of Biochemistry and Biophysics, University of California, Davis, California 95616, USA., Daubert SD, Schneider IR, Bruening G |
| Jazyk: |
angličtina |
| Zdroj: |
Virology [Virology] 1982 Sep; Vol. 121 (2), pp. 262-73. |
| DOI: |
10.1016/0042-6822(82)90166-0 |
| Abstrakt: |
An approximately 350-nucleotide residue RNA replicates in association with tobacco ringspot virus (TobRV) and becomes encapsidated in TobRV coat protein. Here we show by electrophoretic analyses that this small satellite RNA, RNA S, is the most abundant and most rapidly migrating of a series of at least ten encapsidated RNAs with RNA S sequences. A largely double-stranded RNA fraction from infected tissue, when denatured, gave a similar series of up to 12 zones that contained both RNA S sequences and sequences that hybridized to RNA S. Analysis of the mobilities suggests a weight increment between each zone corresponding approximately to the size of RNA S. Thus the more slowly migrating zones appear to contain covalent multimers of RNA S or, for tissue RNA, both multimers of RNA S and multimers of the complement of RNA S sequences. Neither terminal structure of TobRV genomic RNAs was found in the satellite RNA. RNA S lacks detectable polyadenylate or oligoadenylate. Covalently linked protein was not detected in RNA S or its more slowly migrating forms, and satellite RNA biological activity, unlike that of the TobRV RNAs, was not protease sensitive. Polynucleotide kinase catalyzed the phosphorylation of satellite RNAs, indicating free 5'-hydroxyl groups. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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