Strange bedfellows: polyadenylation factors at the promoter

Calvo, Olga; Manley, James L.

doi:10.1101/gad.1093603

Cited by 131 publications

(103 citation statements)

References 45 publications

Supporting

Mentioning

100

Contrasting

Unclassified

Order By: Relevance

“…Many factors involved in 39-end formation and termination also associate with promoter regions (Calvo and Manley 2003). This has been observed in yeast (Bentley 2002;Calvo and Manley 2003;He et al 2003) and humans (Dantonel et al 1997;Venkataraman et al 2005;Swinburne et al 2006;Zhang et al 2007;Glover-Cutter et al 2008;Rozenblatt-Rosen et al 2009), and suggests a cooperation between the transcription initiation and 39-end processing/termination machineries.…”

Section: Trans-acting Factor Dynamics At the Poly(a) Site Affect Tranmentioning

confidence: 94%

“…This has been observed in yeast (Bentley 2002;Calvo and Manley 2003;He et al 2003) and humans (Dantonel et al 1997;Venkataraman et al 2005;Swinburne et al 2006;Zhang et al 2007;Glover-Cutter et al 2008;Rozenblatt-Rosen et al 2009), and suggests a cooperation between the transcription initiation and 39-end processing/termination machineries. One scenario is that this facilitates recruitment of polyadenylation factors to active genes, and that these factors travel with the EC during transcription (e.g., Dantonel et al 1997).…”

Section: Trans-acting Factor Dynamics At the Poly(a) Site Affect Tranmentioning

confidence: 94%

See 1 more Smart Citation

Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

Self Cite

291

326

View full text Add to dashboard Cite

Gene transcription in the cell nucleus is a complex and highly regulated process. Transcription in eukaryotes requires three distinct RNA polymerases, each of which employs its own mechanisms for initiation, elongation, and termination. Termination mechanisms vary considerably, ranging from relatively simple to exceptionally complex. In this review, we describe the present state of knowledge on how each of the three RNA polymerases terminates and how mechanisms are conserved, or vary, from yeast to human.

show abstract

Section: Trans-acting Factor Dynamics At the Poly(a) Site Affect Tranmentioning

confidence: 94%

Section: Trans-acting Factor Dynamics At the Poly(a) Site Affect Tranmentioning

confidence: 94%

Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

Self Cite

291

326

View full text Add to dashboard Cite

show abstract

“…The absence of an additive effect of deletion of these four FLEX sequences suggests that they function in the same pathway. In budding yeast, transcriptional initiation and termination by RNA polymerase II share some common factors (24), and some genes form a loop structure that juxtaposes promoters and terminators (25). Mei4p might recruit general transcription factors directly when it binds to the upstream region of a gene and do so by looping or bending DNA when it binds to the downstream region.…”

Section: Mei4p Binds To Flex Elements Adjacent To Cdc25mentioning

confidence: 99%

Mei4p coordinates the onset of meiosis I by regulating cdc25 ⁺ in fission yeast

Murakami-Tonami

Yamada‐Namikawa

Tochigi

et al. 2007

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

View full text Add to dashboard Cite

The kinase Cdc2p is a central regulator of entry into and progression through nuclear division during mitosis and meiosis in eukaryotes. Cdc2p is activated at the onset of mitosis by dephosphorylation on tyrosine-15, the phosphorylation status of which is determined mainly by the kinase Wee1p and the phosphatase Cdc25p. In fission yeast, the forkhead-type transcription factor Mei4p is required for expression of many genes during meiosis, with mei4 mutant cells arresting before meiosis I. The mechanism of cell cycle arrest in mei4 cells has remained unknown, however. We now show that cdc25 ؉ is an important target of Mei4p in control of entry into meiosis I. Forced dephosphorylation of Cdc2p on tyrosine-15 thus induced meiosis I in mei4 mutant cells without a delay, although no spores were formed. We propose that Mei4p acts as a rate-limiting regulator of meiosis I by activating cdc25 ؉ transcription in coordination with other meiotic events.cell cycle ͉ transcription

show abstract

“…Most eukaryotic messenger RNA precursors (pre-mRNAs) undergo extensive maturational processing, including 3'-end cleavage and polyadenylation [1][2][3][4][5][6][7][8] . Despite the characterization of a large number of proteins that are required for the cleavage reaction, the identity of the endoribonuclease is not known 4,9,10 .…”

Section: Introductionmentioning

confidence: 99%

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

Mandel

Kaneko

Zhang

et al. 2006

Nature

Self Cite

409

524

View full text Add to dashboard Cite

Most eukaryotic messenger RNA precursors (pre-mRNAs) undergo extensive maturational processing, including 3'-end cleavage and polyadenylation [1][2][3][4][5][6][7][8] . Despite the characterization of a large number of proteins that are required for the cleavage reaction, the identity of the endoribonuclease is not known 4,9,10 . Recent analyses suggested that the 73 kD subunit of cleavage and polyadenylation specificity factor (CPSF-73) may be the endonuclease for this and related reactions [10][11][12][13][14][15] , although no direct data confirmed this. Here we report the crystal structures of human CPSF-73 at 2.1 Å resolution, complexed with zinc ions and a sulfate that may mimic the phosphate group of the substrate, and the related yeast protein CPSF-100 (Ydh1p) at 2.5 Å resolution. Both CPSF-73 and CPSF-100 contain two domains, a metallo-β-lactamase domain and a novel β-CASP domain. The active site of CPSF-73, with two zinc ions, is located at the interface of the two domains. Purified recombinant CPSF-73 possesses endoribonuclease activity, and mutations that disrupt zinc binding in the active site abolish this activity. Our studies provide the first direct experimental evidence that CPSF-73 is the pre-mRNA 3'-end processing endonuclease. Keywordspolyadenylation; metallo-β-lactamase; pre-mRNA processing; Artemis; V(D)J recombination; double-strand break repair CPSF-73 belongs to the metallo-β-lactamase superfamily of zinc-dependent hydrolases 11,12 . Canonical metallo-β-lactamases contain five signature sequence motifs-Asp (motif 1), His-X-His-X-Asp-His (motif 2), His (motif 3), Asp (motif 4) and His (motif 5), most of which are ligands to the two zinc ions in their active site. Sequence conservation between CPSF-73 and the canonical metallo-β-lactamases is limited to these signature motifs. While the first four motifs can be identified in the N-terminal segment of CPSF-73 (Supplemental Fig. 1a, Supplemental Table 1), the fifth motif was uncertain, with three candidates, A (Asp or Glu), B (His), and C (His) (Supplemental Fig. 1a), in the so-called β-CASP motif 12 . Motif B was proposed to be equivalent to motif 5 in the canonical metallo-β-lactamases. Another subunit of CPSF, CPSF-100, shares sequence conservation (Supplemental Fig. 1b) Fig. 1a) with CPSF-73 but lacks the putative Zn 2+ binding residues.To understand the roles of CPSF-73 and CPSF-100 in pre-mRNA 3'-end processing, we determined the structures of human CPSF-73 (residues 1-460), and yeast CPSF-100 (residues 1-720) (the crystallographic data are summarized in Supplemental Table 2). The two structures obtained for CPSF-73 were crystallized in the absence or presence of 0.5 mM zinc (although both structures contained zinc atoms; see below). We discovered serendipitously that in situ proteolysis by a fungal protease is crucial for the crystallization of yeast CPSF-100 16 .The structure of CPSF-73 can be divided into two domains (Fig. 1a). The N-terminal residues (amino acids 1-208) form a domain similar to the structure of canonical me...

show abstract

Strange bedfellows: polyadenylation factors at the promoter

Cited by 131 publications

References 45 publications

Transcription termination by nuclear RNA polymerases

Transcription termination by nuclear RNA polymerases

Mei4p coordinates the onset of meiosis I by regulating cdc25 ⁺ in fission yeast

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

Contact Info

Product

Resources

About

Strange bedfellows: polyadenylation factors at the promoter

Cited by 131 publications

References 45 publications

Transcription termination by nuclear RNA polymerases

Transcription termination by nuclear RNA polymerases

Mei4p coordinates the onset of meiosis I by regulating cdc25 + in fission yeast

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

Contact Info

Product

Resources

About

Mei4p coordinates the onset of meiosis I by regulating cdc25 ⁺ in fission yeast