Rous sarcoma virus p19 binds to specific double-stranded regions of viral RNA: Effect of p19 on cleavage of viral RNA by RNase III
The extent of binding of purified RSV(Pr-C) p19 and p12 to a variety of RNAs was measured using a sensitive nitrocellulose filter binding assay which is capable of detecting binding reactions with association constants as low as 3 × 10 6 liters × mol −1 (Hizi, A., Leis, J. P., and Joklik, W. K. 1977...
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Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1978, Vol.84 (1), p.87-98 |
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Sprache: | eng |
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Zusammenfassung: | The extent of binding of purified RSV(Pr-C) p19 and p12 to a variety of RNAs was measured using a sensitive nitrocellulose filter binding assay which is capable of detecting binding reactions with association constants as low as 3 × 10
6 liters × mol
−1 (Hizi, A., Leis, J. P., and Joklik, W. K. 1977). RSV p19 bound 60 and 34 S RSV (Pr-C) RNA with association constants of 5.1 × 10
11 and 1.8 × 10
10 liters × mol
−1. RSV p19 bound preferentially to specific double-stranded regions of the RNA since: (a) The association constant for
Neurospora nuclease-digested 34 S RNA was the same as for untreated RNA; (b) the association constant for 34 S RNA partially digested with
Escherichia coli RNase III (which is specific for double-stranded RNA regions) was 30-fold lower than for untreated RNA; (c) p19 prevented cleavage of 34 S RSV-RNA by
E. coli RNase III; (d) p19 bound cell precursor RNAs containing RNase III-sensitive sites, but not mature RNAs lacking RNase III-sensitive sites. On the other hand, purified RSV p12 bound all RNAs tested with association constants roughly proportional to their molecular weights. A possible function for p19 in regulating the processing of viral RNA and its subsequent translation has been proposed. |
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ISSN: | 0042-6822 1096-0341 |
DOI: | 10.1016/0042-6822(78)90220-9 |