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Human pre-mRNA 3'-end processing machinery database
CF Im - mammalian cleavage factor I
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CF Im is involved in RNA-binding step (recognizes UGUA cassette) . It consists CF Im25 and one of closely realated proteins CF Im59
or CF Im68. Acts as a dimer.
CF Im25 contains Nudix hydrolases domain, but it does not contain catalitic residues and the enzymatic activity. Instead, Nudix-like domain of CF Im25 is responsible for interaction with RNA. Both, CF Im59 and CF Im68 contains RRM domains. Additionaly, they contain also RS domain (rich in arginine/serine dipeptide repeats).
CF Im acts as primary RNA-binding factor of 3' mRNA processing machinery and serves as general scaffold for other proteins. Moreover, CF Im is a component of the spliceosome.
CF Im25 contains Nudix hydrolases domain, but it does not contain catalitic residues and the enzymatic activity. Instead, Nudix-like domain of CF Im25 is responsible for interaction with RNA. Both, CF Im59 and CF Im68 contains RRM domains. Additionaly, they contain also RS domain (rich in arginine/serine dipeptide repeats).
CF Im acts as primary RNA-binding factor of 3' mRNA processing machinery and serves as general scaffold for other proteins. Moreover, CF Im is a component of the spliceosome.
Literature:
- Yang Q, Gilmartin GM, Doublie S et al. et al. The structure of human cleavage factor I(m) hints at functions beyond UGUA-specific RNA binding: a role in alternative polyadenylation and a potential link to 5" capping and splicing. RNA Biol 2011 8(5):748-53, doi: 10.4161/rna.8.5.16040, PMID: 21881408.
- Gruber AR, Martin G, Keller W et al. et al. Cleavage factor Im is a key regulator of 3" UTR length. RNA Biol 2012 9(12):1405-12, doi: 10.4161/rna.22570, PMID: 23187700.
- Ruegsegger U, Beyer K, Keller W et al. et al. Purification and characterization of human cleavage factor Im involved in the 3" end processing of messenger RNA precursors. J Biol Chem 1996 271(11):6107-13, doi: , PMID: 8626397.
- Martin G, Gruber AR, Keller W et al. et al. Genome-wide analysis of pre-mRNA 3" end processing reveals a decisive role of human cleavage factor I in the regulation of 3" UTR length. Cell Rep 2012 1(6):753-63, doi: 10.1016/j.celrep.2012.05.003, PMID: 22813749.
- Mandel CR, Bai Y, Tong L et al. et al. Protein factors in pre-mRNA 3"-end processing. Cell Mol Life Sci 2008 65(7-8):1099-122, doi: 10.1007/s00018-007-7474-3, PMID: 18158581.
- Yang Q, Doublie S.. Structural biology of poly(A) site definition. Wiley Interdiscip Rev RNA 2011 2(5):732-47, doi: 10.1002/wrna.88, PMID: 21823232.
- Shi Y, Di Giammartino DC, Taylor D et al. et al. Molecular architecture of the human pre-mRNA 3" processing complex. Mol Cell 2009 33(3):365-76, doi: 10.1016/j.molcel.2008.12.028, PMID: 19217410.
Contact: Lukasz Kozlowski
This work was supported by Polish Ministry of Science and Higher Education (grant NN301 190139).
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