Distinct Sequence Motifs within the 68-kDa Subunit of Cleavage Factor I m Mediate RNA Binding, Protein-Protein Interactions, and Subcellular Localization *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 279, Issue: 34, Page: 35788-35797
2004
- 125Citations
- 105Captures
- 11Mentions
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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
- Citations125
- Citation Indexes125
- 125
- CrossRef109
- Captures105
- Readers105
- 105
- Mentions11
- References11
- 11
Article Description
Cleavage factor I m (CF I m ) is required for the first step in pre-mRNA 3′-end processing and can be reconstituted in vitro from its heterologously expressed 25- and 68-kDa subunits. The binding of CF I m to the pre-mRNA is one of the earliest steps in the assembly of the cleavage and polyadenylation machinery and facilitates the recruitment of other processing factors. We identified regions in the subunits of CF I m involved in RNA binding, protein-protein interactions, and subcellular localization. CF I m 68 has a modular domain organization consisting of an N-terminal RNA recognition motif and a C-terminal alternating charge domain. However, the RNA recognition motif of CF I m 68 on its own is not sufficient to bind RNA but is necessary for association with the 25-kDa subunit. RNA binding appears to require a CF I m 68/25 heterodimer. Whereas multiple protein interactions with other 3′-end-processing factors are detected with CF I m 25, CF I m 68 interacts with SRp20, 9G8, and hTra2β, members of the SR family of splicing factors, via its C-terminal alternating charge domain. This domain is also required for targeting CF I m 68 to the nucleus. However, CF I m 68 does not concentrate in splicing speckles but in foci that partially colocalize with paraspeckles, a subnuclear component in which other proteins involved in transcriptional control and RNA processing have been found.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820731650; http://dx.doi.org/10.1074/jbc.m403927200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=4143151952&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15169763; http://www.jbc.org/lookup/doi/10.1074/jbc.M403927200; https://syndication.highwire.org/content/doi/10.1074/jbc.M403927200; https://linkinghub.elsevier.com/retrieve/pii/S0021925820731650; https://dx.doi.org/10.1074/jbc.m403927200
American Society for Biochemistry & Molecular Biology (ASBMB)
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