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

Benoit, Béatrice; Juge, François; Iral, Florence; Audibert, Agnès; Simonelig, Martine

doi:10.1073/pnas.162191899

Cited by 17 publications

(21 citation statements)

References 48 publications

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“…The crystal structure of the HAT domain revealed an intrinsic dimeric association ( Fig. 2B) (84,85), which is consistent with earlier biochemical characterizations (35), as well as genetic studies with flies (86), suggesting that CstF assembles with two copies of each subunit (84). Similar characteristics have also been observed in the fungal homolog of CstF-77, Rna14.…”

Section: Cstfsupporting

confidence: 88%

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Xiang

Tong

Manley

2014

Molecular and Cellular Biology

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Processing of mRNA precursors (pre-mRNAs) by polyadenylation is an essential step in gene expression. Polyadenylation consists of two steps, cleavage and poly(A) synthesis, and requires multiple cis elements in the pre-mRNA and a megadalton protein complex bearing the two essential enzymatic activities. While genetic and biochemical studies remain the major approaches in characterizing these factors, structural biology has emerged during the past decade to help understand the molecular assembly and mechanistic details of the process. With structural information about more proteins and higher-order complexes becoming available, we are coming closer to obtaining a structural blueprint of the polyadenylation machinery that explains both how this complex functions and how it is regulated and connected to other cellular processes.

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Section: Cstfsupporting

confidence: 88%

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Xiang

Tong

Manley

2014

Molecular and Cellular Biology

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“…This dimerization is supported by studies in solution, yeast two-hybrid assays [152], far Western experiments [141], as well as by solution and electron microscopy studies on Rna14p [155]. In addition, self-association of CstF-77 has been suggested based on genetic observations on the Drosophila homolog Su(f), as distinct lethal alleles of Su(f) can partially complement each other [150,156]. Taken together, these data suggest that CstF-77 may function as a dimer at a crucial stage in pre-mRNA 3′-end processing.…”

Section: Cstf-77 (Rna14p)mentioning

confidence: 88%

“…Mutation of the Drosophila homolog of CstF-77, suppressor of forked su(f), results in the utilization of alternative poly(A) sites [149]. This defect can be rescued by the addition of human CstF-77 [150].…”

Section: Cstf-77 (Rna14p)mentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

355

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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“…In vitro interactions were performed as described (Benoit et al, 2002), in the presence of 0.2 μg/μl RNase A. Orb was in vitro translated from the orb D5 cDNA cloned into pBluescript using EcoRI and HindIII.…”

Section: Gst Pull-down Assaysmentioning

confidence: 99%

PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis inDrosophila

et al. 2008

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*Cytoplasmic polyadenylation has an essential role in activating maternal mRNA translation during early development. In vertebrates, the reaction requires CPEB, an RNA-binding protein and the poly(A) polymerase GLD-2. GLD-2-type poly(A) polymerases form a family clearly distinguishable from canonical poly(A) polymerases (PAPs). In Drosophila, canonical PAP is involved in cytoplasmic polyadenylation with Orb, the Drosophila CPEB, during mid-oogenesis. We show that the female germline GLD-2 is encoded by wispy. Wispy acts as a poly(A) polymerase in a tethering assay and in vivo for cytoplasmic polyadenylation of specific mRNA targets during late oogenesis and early embryogenesis. wispy function is required at the final stage of oogenesis for metaphase of meiosis I arrest and for progression beyond this stage. By contrast, canonical PAP acts with Orb for the earliest steps of oogenesis. Both Wispy and PAP interact with Orb genetically and physically in an ovarian complex. We conclude that two distinct poly(A) polymerases have a role in cytoplasmic polyadenylation in the female germline, each of them being specifically required for different steps of oogenesis.

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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

Cited by 17 publications

References 48 publications

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Delineating the Structural Blueprint of the Pre-mRNA 3′-End Processing Machinery

Protein factors in pre-mRNA 3′-end processing

PAP- and GLD-2-type poly(A) polymerases are required sequentially in cytoplasmic polyadenylation and oogenesis inDrosophila

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