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Human pre-mRNA 3'-end processing machinery database
CstF - cleavage stimulation factor complex
CstF recognizes U/GU-rich downstream cassette and is
required only for cleavege of mRNA. The RNA-binding is mediated by N-teminal RRM domain of CstF64/CstF64tau. Additionaly, CPSF binded to A(A/U)UAAA stabilizes this interaction. Tau
version of CstF64 has similar structure, but its RNA specificity is slightly different. Moreover, it is highly expressed only in the testis. CstF77 serves as general scaffolding component.
CstF50 can dimerize through its N teminal domain. The rest of protein is occupied by WD-40 domains mediating protein-protein interactions. CstF50 interacts with C teminal domain of RNA polimerase II (RPB1).
Literature:
- Moreno-Morcillo M, Minvielle-Sebastia L, Mackereth C et al. et al. Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure. RNA 2011 17(3):412-8, doi: 10.1261/rna.2481011, PMID: 21233223.
- Ruepp MD, Schweingruber C, Kleinschmidt N et al. et al. Interactions of CstF-64, CstF-77, and symplekin: implications on localisation and function. Mol Biol Cell 2011 22(1):91-104, doi: 10.1091/mbc.E10-06-0543, PMID: 21119002.
- Nag A, Narsinh K, Martinson HG et al. et al. The poly(A)-dependent transcriptional pause is mediated by CPSF acting on the body of the polymerase. Nat Struct Mol Biol 2007 14(7):662-9, doi: 10.1038/nsmb1253, PMID: 17572685.
- Legrand P, Pinaud N, Minvielle-Sebastia L et al. et al. The structure of the CstF-77 homodimer provides insights into CstF assembly. Nucleic Acids Res 2007 35(13):4515-22, doi: 10.1093/nar/
gkm458, PMID: 17584787.
- 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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