| Autor: |
Heywood, Stuart M., Kennedy, Doris S., Bester, André J. |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; Oct75 Part 2, Vol. 58 Issue 2, p587-593, 7p |
| Abstrakt: |
Muscle translational-control RNA (tcRNA) has been separated into two classes, polysomal and messenger ribonuclear protein (mRNA · protein), which have different sizes as determined by acrylamide gel electrophoresis. While normally translation of mRNA · protein mRNA is inhibited by tcRNA derived from the same mRNA · proteins, this inhibition does not occur if the messenger is previously de-adenylated. This suggests that the poly(A) segment of mRNA is required for the tcRNA activity. Utilizing different mRNA · protein fractions from muscle, myosin mRNA · protein and small mRNA proteins (< 30 S), we have been able to demonstrate that a degree of specificity exists in the interaction of tcRNA and mRNA derived from the same mRNA · proteins. This is illustrated by the facts that (a) each tcRNA only inhibits the translation of its respective mRNA and (b) the highest percentage of structural change occurs when each tcRNA is hybridized to its respective mRNA as measured by its resistance to T1 and T2 RNase. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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