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Cleavage stimulation factor, 3' pre-RNA, subunit 3, 77kDa

CstF-77, CSTF3
The protein encoded by this gene is one of three (including CSTF1 and CSTF2) cleavage stimulation factors that combine to form the cleavage stimulation factor complex (CSTF). This complex is involved in the polyadenylation and 3' end cleavage of pre-mRNAs. The encoded protein functions as a homodimer and interacts directly with both CSTF1 and CSTF2 in the CSTF complex. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CstF-64, CAN, STEP, CPSF, POLYMERASE
Papers on CstF-77
A novel Alu-mediated microdeletion at 11p13 removes WT1 in a patient with cryptorchidism and azoospermia.
Lopes et al., Porto, Portugal. In Reprod Biomed Online, 2014
It was confirmed by multiplex ligation-dependent probe amplification that this heterozygous deletion spanned nine genes (WT1, EIF3M, CCDC73, PRRG4, QSER1, DEPDC7, TCP11L1, CSTF3 and HIPK3) and positioned the breakpoints within highly homologous repetitive elements.
3' end formation of pre-mRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells.
West et al., Edinburgh, United Kingdom. In Genes Dev, 2014
We found that the CTD is heavily phosphorylated on Ser2 (Ser2p) at poly(A) (pA) signals coincident with recruitment of the CstF77 CPA factor.
The conserved intronic cleavage and polyadenylation site of CstF-77 gene imparts control of 3' end processing activity through feedback autoregulation and by U1 snRNP.
Tian et al., Newark, United States. In Plos Genet, 2012
The human gene encoding the cleavage/polyadenylation (C/P) factor CstF-77 contains 21 exons.
Crystal structure of the Rna14-Rna15 complex.
Tong et al., New York City, United States. In Rna, 2012
These two proteins are homologs of CstF-77 and CstF-64 in the cleavage stimulation factor (CstF) of the mammalian 3'-end processing machinery.
Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.
Fribourg et al., Pessac, France. In Rna, 2011
Together with previous data on the structure of CstF-77, homodimerization of CstF-50 N-terminal domain supports the model in which the functional state of CstF is a heterohexamer.
Interactions of CstF-64, CstF-77, and symplekin: implications on localisation and function.
Schümperli et al., Bern, Switzerland. In Mol Biol Cell, 2011
nuclear accumulation of CstF-64 depends on binding to CstF-77 not symplekin; interaction between CstF-64/CstF-64Tau and CstF-77 are important for maintenance of nuclear levels of CstF complex components and intracellular localization, stability, function
The Arabidopsis ortholog of the 77 kDa subunit of the cleavage stimulatory factor (AtCstF-77) involved in mRNA polyadenylation is an RNA-binding protein.
Hunt et al., Lexington, United States. In Febs Lett, 2010
The 77 kDa subunit of the polyadenylation cleavage stimulation factor (CstF77) is important in messenger RNA 3' end processing.
Targeted 3' processing of antisense transcripts triggers Arabidopsis FLC chromatin silencing.
Dean et al., Norwich, United Kingdom. In Science, 2010
Through suppressor mutagenesis, we identify a requirement for CstF64 and CstF77, two conserved RNA 3'-end-processing factors, in FLC silencing.
The hinge domain of the cleavage stimulation factor protein CstF-64 is essential for CstF-77 interaction, nuclear localization, and polyadenylation.
MacDonald et al., Lubbock, United States. In J Biol Chem, 2010
The Hinge domain is necessary for CstF-64 interaction with CstF-77 and consequent nuclear localization.
Crystal structure of murine CstF-77: dimeric association and implications for polyadenylation of mRNA precursors.
Tong et al., New York City, United States. In Mol Cell, 2007
Crystal structure of the HAT (half a TPR) domain of murine CstF-77, as well as its C-terminal subdomain.
The use of in situ proteolysis in the crystallization of murine CstF-77.
Tong et al., New York City, United States. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007
During structure determination of the 77 kDa subunit of the murine CstF complex (CstF-77), it was serendipitously discovered that a solution infected by a fungus was crucial for the crystallization of this protein.
The structure of the CstF-77 homodimer provides insights into CstF assembly.
Fribourg et al., Bordeaux, France. In Nucleic Acids Res, 2006
Mapping experiments identify the C-terminal region of Rna14p, the yeast counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.
Identification of DDX1 as a JC virus transcriptional control region-binding protein.
Sawa et al., Sapporo, Japan. In Microbiol Immunol, 2006
We performed a yeast two-hybrid assay using CstF-77 as the bait against a HeLa cDNA-subtracted IMR-32 cDNA library.
Cytoplasmic CstF-77 protein belongs to a masking complex with cytoplasmic polyadenylation element-binding protein in Xenopus oocytes.
Mandart et al., Montpellier, France. In J Biol Chem, 2006
However, some evidence suggests that the CstF-77 subunit might have a function independent of nuclear polyadenylation, which could be related to the cell cycle.
Chimeric human CstF-77/Drosophila Suppressor of forked proteins rescue suppressor of forked mutant lethality and mRNA 3' end processing in Drosophila.
Simonelig et al., Montpellier, France. In Proc Natl Acad Sci U S A, 2002
chimeric human CstF-77/Drosophila suppressor of forked proteins rescue suppressor of forked mutant lethality and mrna 3' end processing in Drosophila
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