Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease

Mandel, Corey R.; Kaneko, Syuzo; Zhang, Hailong; Gebauer, Damara; Vethantham, Vasupradha; Manley, James L.; Tong, Liang

doi:10.1038/nature05363

Cited by 409 publications

(554 citation statements)

References 31 publications

(39 reference statements)

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“…The crystal structure of the metallo-β-lactamase and β-CASP domains of Cft2p/Ydh1p was reported recently [112]. The overall structure is similar to that of CPSF-73 (Fig.…”

Section: Cpsf-100 (Cft2p/ydh1p)supporting

confidence: 59%

“…Biochemical studies with the bacterially expressed and purified human CPSF-73 showed that it possessed weak ribonuclease activity towards pre-mRNA substrates [112], in the absence of the other proteins of the 3′-end processing machinery. This activity was enhanced greatly when the purified protein was pre-incubated with Ca 2+ ions.…”

Section: Cpsf-73 (Brr5p/ysh1p)mentioning

confidence: 99%

“…The exact function of this protein in 3′-end processing is currently not known. Cft2p/Ydh1p contains an insert of about 200 residues (residues 401-601) that is highly charged and hydrophilic [112], which explains its larger size compared to CPSF-73 but the functional role of this segment is not known. CPSF-100 contains a similar (though shorter) segment (Fig.…”

Section: Cpsf-100 (Cft2p/ydh1p)mentioning

confidence: 99%

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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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“…The crystal structure of the metallo-β-lactamase and β-CASP domains of Cft2p/Ydh1p was reported recently [112]. The overall structure is similar to that of CPSF-73 (Fig.…”

Section: Cpsf-100 (Cft2p/ydh1p)supporting

confidence: 59%

Section: Cpsf-73 (Brr5p/ysh1p)mentioning

confidence: 99%

Section: Cpsf-100 (Cft2p/ydh1p)mentioning

confidence: 99%

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Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

364

482

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“…The former is bound by the cleavage and polyadenylation specificity factor (CPSF) complex and the latter by cleavage stimulation factors (CstF). The RNA is then cut by CPSF73 [3], whereupon the coding portion is polyadenylated and the 3ʹ product rapidly degraded. The central role of the PAS in termination provides the premise for two potential mechanisms.…”

Section: Overviewmentioning

confidence: 99%

An end in sight? Xrn2 and transcriptional termination by RNA polymerase II

Eaton

West

2018

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“…The b-CASP domain, which is always appended to a metallo-blactamase domain, is strictly required for Artemis function (Poinsignon et al, 2004b). The three-dimensional structure of several RNA-specific b-CASP members has recently revealed the general organization of these proteins into two domains: a metallo-b-lactamase domain and a b-CASP domain, with the active site being located at the interface between the two domains (Ishikawa et al, 2006;Mandel et al, 2006). Several Serine residues, mostly located in the C-terminus half of the protein, have been identified in vitro and in vivo as targets of phosphatidylinositol 3-kinase like kinases, including DNA-PKcs (Poinsignon et al, 2004a; Riballo et al, 2004;Zhang et al, 2004;Chen et al, 2005;Ma et al, 2005;Wang et al, 2005b;Goodarzi et al, 2006;Soubeyrand et al, 2006).…”

Section: Artemismentioning

confidence: 99%

V(D)J and immunoglobulin class switch recombinations: a paradigm to study the regulation of DNA end-joining

et al. 2007

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The immune system is the site of intense DNA damage/ modification, which occur during the development and maturation of B and T lymphocytes. V(D)J recombination is initiated by the Rag1 and Rag2 proteins and the formation of a DNA double-strand break (DNA dsb). This DNA lesion is repaired through the use of the nonhomologous end-joining (NHEJ) pathway, several factors of which have been identified through the survey of immunodeficient conditions in humans and mice. Upon antigenic recognition in secondary lymphoid organs, mature B cells further diversify their repertoire through class switch recombination (CSR). CSR is a region-specific rearrangement process triggered by the activation-induced cytidine deaminase factor and also proceeds through the introduction of DNA dsb. However, unlike V(D)J recombination, CSR does not rely strictly on NHEJ for the repair of the DNA lesion. Instead, CSR, but not V(D)J recombination, requires the major factors of the DNA damage response. V(D)J recombination and CSR thus represent an interesting paradigm to study the regulation among the various DNA repair pathways. Oncogene (2007) 26, 7780-7791; doi:10.1038/sj.onc.1210875 Keywords: V(D)J recombination; class switch recombination; SCID; Artemis; Cernunnos; NHEJ V(D)J recombination and CSR: two rearrangement processes that shape the immune system repertoire B and T lymphocytes respond to foreign pathogens through specialized antigenic receptors, the B-cell receptor and T-cell receptor, respectively. The required diversity of these receptors is ensured by the V(D)J recombination process (Figure 1) which assembles previously scattered Variable (V), Diversity (D) and Joining (J) encoding gene segments through a specialized somatic DNA rearrangement mechanism (Tonegawa, 1983). The reaction is initiated by the lymphoid-specific factors, Rag1 and Rag2, which recognize recombination signal sequences (RSS) that flank all V, D and J gene units and introduce a DNA dsb at the border of the RSS (see Dudley et al. (2005) for a review on V(D)J recombination). The resulting DNA double-strand break (DNA dsb) is resolved by the ubiquitous DNA repair machinery known as non-homologous end-joining (NHEJ). The convergent efforts of scientists in the immunology and DNA repair fields were decisive in defining the various actors and molecular mechanisms of this DNA repair pathway over the years as will be discussed below.The terminal maturation of B lymphocytes, which occurs in germinal centres of secondary lymphoid organs upon antigen recognition, is accompanied by two additional molecular processing of immunoglobulin genes that increase the efficiency of the humoral response: (1) the class switch recombination (CSR, Figure 2) exchanges the immunoglobulin (Ig) constant region (CH), thus modifying the function of the Ig without altering its antigenic specificity (Manis et al., 2002b) and (2) somatic hypermutations are introduced in the Ig variable domains, thus increasing their affinity for antigen (Papavasiliou and Schatz, 2002). These two events ar...

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Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease

Cited by 409 publications

References 31 publications

Protein factors in pre-mRNA 3′-end processing

Protein factors in pre-mRNA 3′-end processing

An end in sight? Xrn2 and transcriptional termination by RNA polymerase II

V(D)J and immunoglobulin class switch recombinations: a paradigm to study the regulation of DNA end-joining

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