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Cleavage stimulation factor subunit 1
Known also as: CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit
Known abbreviations: CSTF1, CstF-50, CstFp50
Yeast homolog: not known
Protein
Models Domains Secondary structure Disorder |
Top 3 models:
 |  |  |
| Template: 1nr0, chain A Method: hhsearch Fragment: 5-111 | Template: 4ery, chain A Method: pdbblast Fragment: 104-432 | Template: 1nr0, chain A Method: phyre Fragment: 4-425 |
| Sequence length: | 431 aa |
| Molecular weight: | 48.358 kDa |
| Isoelectric point: | 6.3 |
Sequence:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MYRTKVGLKDRQQLYKLIISQLLYDGYISIANGLINEIKPQSVCAPSEQLLHLIKLGMENDDTAVQYAIGRSDTVAPGTGIDLEFDADVQTMSPEASEYETCYVTSHKGPCRVATYSRDGQLIATGSADA
SIKILDTERMLAKSAMPIEVMMNETAQQNMENHPVIRTLYDHVDEVTCLAFHPTEQILASGSRDYTLKLFDYSKPSAKRAFKYIQEAEMLRSISFHPSGDFILVGTQHPTLRLYDINTFQCFVSCNPQDQ
HTDAICSVNYNSSANMYVTGSKDGCIKLWDGVSNRCITTFEKAHDGAEVCSAIFSKNSKYILSSGKDSVAKLWEISTGRTLVRYTGAGLSGRQVHRTQAVFNHTEDYVLLPDERTISLCCWDSRTAERRN
LLSLGHNNIVRCIVHSPTNPGFMTCSDDFRARFWYRRSTTD
Gene location: 20q13.2
Summary
One of the protein of CSTF complex. Required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA.
It contains seven WD-40 repeats that begin about 90 residues from the N-terminus . The WD-40 repeats are required for interaction with CstF-77, and deletion of the last repeat reduces binding. CstF-50 also can self-associate and only the N-terminal region is required for this interaction. CstF-50 does not appear to have a sequence homolog in yeast.
WD6 repeat of CstF-50 interacts with protein BARD1, which associates with the tumor suppressor BRCA1. This interaction inhibits 3?-end cleavage of pre-mRNAs in vitro.
WD domains are responsible for interaction with CSTF3. Similar to mammalian G protein beta subunits, this protein contains transducin-like repeats.
Both CstF-50 and CstF-77 bind specifically to the CTD of PolII but CstF-50 binds with a higher efficiency. This binding is significantly reduced upon deletion of the first 91 amino acids of CstF-50, indicating that the WD-40 repeats are not sufficient for interaction. RNAi experiments showed that CstF-50 also interacts with the splicing co-activator SRm160, establishing another link between 3?-end processing and transcription.
Interacts directly with CSTF3.
Interacts with BARD1.
Acts as homodimer (N-terminus mediates homodimerization).
See this protein in other databases:
Literature:
- Kleiman FE, Manley JL. Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50. Science 1999 285(5433):1576-9, doi: , PMID: 10477523.
- Takagaki Y, Manley JL. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol Cell Biol 2000 20(5):1515-25, doi: , PMID: 10669729.
- Kleiman FE, Manley JL. The BARD1-CstF-50 interaction links mRNA 3" end formation to DNA damage and tumor suppression. Cell 2001 104(5):743-53, doi: , PMID: 11257228.
- Edwards RA, Lee MS, Tsutakawa SE et al. The BARD1 C-terminal domain structure and interactions with polyadenylation factor CstF-50. Biochemistry 2008 47(44):11446-56, doi: 10.1021/bi801115g, PMID: 18842000.
- Moreno-Morcillo M, Minvielle-Sebastia L, Mackereth C 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.
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