Affiliation:
1. School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Abstract
Ty elements of
Saccharomyces cerevisiae
are long terminal repeat (LTR) retroelements related to retroviruses. Normal levels of Ty1 transposition require Dbr1p, a cellular enzyme that cleaves 2′–5′ RNA bonds. We show that Ty1 RNAs lacking identifiable 5′ ends accumulate in virus-like particles (VLPs) in
dbr1
mutants. Debranching this RNA in vitro with Dbr1p creates an uncapped version of the normal Ty1 RNA 5′ end. We show that the 5′ nucleotide (nt) of Ty1 RNA forms a 2′–5′ bond witha nt near the 3′ end of the same RNA, creating a lariat. The properties of the lariat suggest it forms by a novel mechanism and that branching and debranching may play roles in Ty1 reverse transcription at the minus-strand transfer step.
Publisher
American Association for the Advancement of Science (AAAS)
Reference24 articles.
1. J. Boeke, J. Stoye, in Retroviruses, J. Coffin, S. Hughes, H. Varmus, Eds. (Cold Spring Harbor Laboratory Press, Plainview, NY, 1997), pp. 343–435.
2. Isolation and characterization of the gene encoding yeast debranching enzyme
3. The Yeast Retrotransposons Ty1 and Ty3 Require the RNA Lariat Debranching Enzyme, Dbr1p, for Efficient Accumulation of Reverse Transcripts
4. Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae.
5. Relationship between RNA Lariat Debranching and Ty1 Element Retrotransposition
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