Protein-dependent splicing of a group I intron in ribonucleoprotein particles and soluble fractions
Cell, ISSN: 0092-8674, Vol: 46, Issue: 5, Page: 669-680
1986
- 51Citations
- 9Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations51
- Citation Indexes51
- 51
- CrossRef44
- Captures9
- Readers9
Article Description
The group I intron in the Neurospora mitochondrial large rRNA gene is not self-splicing in vitro. Here, we show that this intron can be spliced from 35S pre-rRNA in RNPs or from deproteinized 35S pre-rRNA or in vitro transcripts by a soluble activity that is present in mitochondrial lysates and can be released from RNPs. Splicing occurs by the same guanosine-initiated transesterification mechanism characteristic of self-splicing group I introns, but is absolutely dependent upon proteins that are presumably required for correct folding of the pre-rRNA. The soluble splicing activity is not simply associated with large subunit ribosomal proteins. Nuclear mutant cyt18-1, which is defective in splicing a number of group I introns in vivo, is grossly deficient in the soluble splicing activity. Our results suggest that the cyt18 gene encodes or regulates a component of an activity that functions in splicing group I introns in Neurospora mitochondria.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0092867486903429; http://dx.doi.org/10.1016/0092-8674(86)90342-9; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0023058976&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/2427199; https://linkinghub.elsevier.com/retrieve/pii/0092867486903429; http://dx.doi.org/10.1016/0092-8674%2886%2990342-9; https://dx.doi.org/10.1016/0092-8674%2886%2990342-9
Elsevier BV
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