RNA Recognition by the Human Polyadenylation Factor CstF

Takagaki, Yoshio; Manley, James L.

doi:10.1128/mcb.17.7.3907

Cited by 197 publications

(240 citation statements)

References 47 publications

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“…GST fusion proteins were generated from Su(f), Drosophila CstF-64, and Drosophila CstF-50. The domains responsible for interaction within CstF were determined in human CstF-64 and CstF-50 proteins in vitro (41). The domain in CstF-64 that mediates interaction with CstF-77 was shown to be a domain called ''hinge,'' located between a ribonucleoprotein-type RNA binding domain and a long proline͞glycine-rich region.…”

Section: Resultsmentioning

confidence: 99%

“…Protein interactions within mammalian CstF have been analyzed in vitro (41). CstF-77 was shown to interact with itself and the other two subunits of the complex, and the domain responsible for these interactions was identified as the internal region containing the proline-rich domain and the short hinge region upstream of it (41). The proline-rich domain alone was shown to interact with CstF-64 and the proline-rich domain in addition to the hinge region was shown to mediate interaction with CstF-50 and CstF-77.…”

Section: Resultsmentioning

confidence: 99%

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Chimeric human CstF-77/ Drosophila Suppressor of forked proteins rescue suppressor of forked mutant lethality and mRNA 3′ end processing in Drosophila

Benoit

Juge

Iral

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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The Suppressor of forked [Su(f)] protein is the Drosophila homologue of CstF-77, a subunit of human cleavage stimulation factor (CstF) that is required for the first step of the mRNA 3 end processing reaction in vitro. We have addressed directly the role of su(f) in the mRNA 3 end processing reaction in vivo. We show that su(f) is required for the cleavage of pre-mRNA during mRNA 3 end formation. Analysis of the functional complementation between Su(f) and CstF-77 shows that most of the Drosophila protein (85%) can be exchanged for the human protein to produce chimeric CstF-77͞Su(f) proteins that rescue lethality and cleavage defect during mRNA 3 end formation in su(f) mutants. Interestingly, we show that a domain in human CstF-77 is limiting for the rescue and that this domain is not able to reproduce protein interactions with the CstF subunits of Drosophila. We also show that chimeric CstF-77͞Su(f) proteins that rescue lethality of su(f) mutants cannot restore utilization of a regulated poly(A) site in Drosophila. Taken together, these results demonstrate that CstF-77 and Su(f) have the same function in mRNA 3 end formation in vivo, but that these two proteins are not interchangeable for regulation of poly(A) site utilization.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Chimeric human CstF-77/ Drosophila Suppressor of forked proteins rescue suppressor of forked mutant lethality and mRNA 3′ end processing in Drosophila

Benoit

Juge

Iral

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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“…For example, for some mammalian polyadenylation factors, such as CstF50, no counterpart could be identified in yeast. 26 In trypanosomes, only Fip1 and CPSF30 had previously been identified and functionally described so far. 8,9 Specifically, CPSF30 is required for polycistronic mRNA processing.…”

Section: Discussionmentioning

confidence: 99%

The polyadenylation complex ofTrypanosoma brucei:Characterization of the functional poly(A) polymerase

et al. 2016

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The generation of mature mRNA in the protozoan parasite Trypanosoma brucei requires coupled polyadenylation and trans splicing. In contrast to other eukaryotes, we still know very little on components, mechanisms, and dynamics of the 3 0 end-processing machinery in trypanosomes. To characterize the catalytic core of the polyadenylation complex in T. brucei, we first identified the poly(A) polymerase [Tb927.7.3780] as the major functional, nuclear-localized enzyme in trypanosomes. In contrast, another poly(A) polymerase, encoded by an intron-containing gene [Tb927.3.3160], localizes mainly in the cytoplasm and appears not to be functional in general 3 0 end processing of mRNAs. Based on tandemaffinity purification with tagged CPSF160 and mass spectrometry, we identified ten associated components of the trypanosome polyadenylation complex, including homologues to all four CPSF subunits, Fip1, CstF50/64, and Symplekin, as well as two hypothetical proteins. RNAi-mediated knockdown revealed that most of these factors are essential for growth and required for both in vivo polyadenylation and trans splicing, arguing for a general coupling of these two mRNA-processing reactions.

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“…The DSE is generally located within 30 nucleotides of the cleavage site (Fig. 1A), although in a few instances DSEs have been observed further downstream [49].…”

Section: The Downstream Element (Dse)-mentioning

confidence: 99%

“…The RRM alone is sufficient for RNA binding and shows preference for the G/Urich DSE (Fig. 1A) [49]. The structure of the RRM of CstF-64 has been determined by NMR (Fig.…”

Section: Cstf-64 (Rna15p)mentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

364

482

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Most eukaryotic mRNA precursors (pre-mRNAs) must undergo extensive processing, including cleavage and polyadenylation at the 3′-end. Processing at the 3′-end is controlled by sequence elements in the pre-mRNA (cis elements) as well as protein factors. Despite the seeming biochemical simplicity of the processing reactions, more than 14 proteins have been identified for the mammalian complex, and more than 20 proteins have been identified for the yeast complex. The 3′-end processing machinery also has important roles in transcription and splicing. The mammalian machinery contains several sub-complexes, including cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF), cleavage factor I (CF I m ), and cleavage factor II (CF II m ). Additional protein factors include poly(A) polymerase (PAP), poly(A) binding protein (PABP), symplekin, and the C-terminal domain (CTD) of RNA polymerase II largest subunit. The yeast machinery includes cleavage factor IA (CF IA), cleavage factor IB (CF IB), and cleavage and polyadenylation factor (CPF).

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RNA Recognition by the Human Polyadenylation Factor CstF

Cited by 197 publications

References 47 publications

Chimeric human CstF-77/ Drosophila Suppressor of forked proteins rescue suppressor of forked mutant lethality and mRNA 3′ end processing in Drosophila

Chimeric human CstF-77/ Drosophila Suppressor of forked proteins rescue suppressor of forked mutant lethality and mRNA 3′ end processing in Drosophila

The polyadenylation complex ofTrypanosoma brucei:Characterization of the functional poly(A) polymerase

Protein factors in pre-mRNA 3′-end processing

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