Abstract
A ∼50-kDa protein binds specifically to the 3′ terminus of 135-nucleotide Drosophila pre-5 S RNA. Unlabeled poly(U) competes out protein binding and stimulates the activity of a 3′-exonuclease, which eventually degrades the substrate to 120 nucleotides, the size of mature 5 S RNA. In its RNA binding and UV cross-linking properties, the endogenous poly(U)-binding protein resembles human La, an autoantigen that binds the U>3 3′ ends of vertebrate RNA polymerase III primary transcripts. This protein appears to inhibit a 3′ exonuclease and could protect 5 S RNA for faithful processing and transport.
Original language | English |
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Pages (from-to) | 11553-11557 |
Number of pages | 5 |
Journal | Journal of Biological Chemistry |
Volume | 268 |
Issue number | 16 |
Publication status | Published - Jun 5 1993 |
Externally published | Yes |
ASJC Scopus Subject Areas
- Biochemistry
- Molecular Biology
- Cell Biology