Protein factors in pre-mRNA 3′-end processing

Mandel, Corey R.; Bai, Yun; Tong, Liang

doi:10.1007/s00018-007-7474-3

Cited by 351 publications

(472 citation statements)

References 233 publications

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“…Other factors were also shown to be required for in vitro 39-end processing, such as cleavage factors I and II (CFI/II). For detailed accounts and a literature survey on this 39-end processing mechanism, see many comprehensive reviews (Colgan and Manley 1997;Zhao et al 1999;Edmonds 2002;Mandel et al 2008;Millevoi and Vagner 2010). Slightly later, budding yeast biochemical characterization of mRNA 39-end processing was achieved.…”

Section: Polyadenylation Signals and 39 Noncoding Rna (Ncrna) Sequencesmentioning

confidence: 99%

“…Whole-cell extracts isolated from yeast strains lacking particular factors (through growth of temperature-sensitive mutants at restrictive temperature) proved valuable in pinning down particular 39-end processing functions. Adding back recombinant factors lacking particular protein domains further uncovered the surprising complexity of this process (Zhao et al 1999;Mandel et al 2008). Why upward of 50 polypeptides divided between multiple subcomplexes are required to simply cleave the pre-mRNA 39 end and then couple poly(A) addition remains an enigma to this day.…”

Section: Polyadenylation Signals and 39 Noncoding Rna (Ncrna) Sequencesmentioning

confidence: 99%

“…In more recent years, biochemists and structural biologists have got their teeth into the molecular characterization of many of the components of the mRNA 39-end processing reaction, and details of these studies are reviewed elsewhere (e.g., Mandel et al 2008). However, a key feature of this reaction is the actual endoribonuclease activity itself, and I outline here the experiments that have led to our current state of understanding of this process.…”

Section: Polyadenylation Signals and 39 Noncoding Rna (Ncrna) Sequencesmentioning

confidence: 99%

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Ending the message: poly(A) signals then and now

Proudfoot¹

2011

Genes Dev.

501

477

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Polyadenylation [poly(A)] signals (PAS) are a defining feature of eukaryotic protein-coding genes. The central sequence motif AAUAAA was identified in the mid1970s and subsequently shown to require flanking, auxiliary elements for both 39-end cleavage and polyadenylation of premessenger RNA (pre-mRNA) as well as to promote downstream transcriptional termination. More recent genomic analysis has established the generality of the PAS for eukaryotic mRNA. Evidence for the mechanism of mRNA 39-end formation is outlined, as is the way this RNA processing reaction communicates with RNA polymerase II to terminate transcription. The widespread phenomenon of alternative poly(A) site usage and how this interrelates with pre-mRNA splicing is then reviewed. This shows that gene expression can be drastically affected by how the message is ended. A central theme of this review is that while genomic analysis provides generality for the importance of PAS selection, detailed mechanistic understanding still requires the direct analysis of specific genes by genetic and biochemical approaches.

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Section: Polyadenylation Signals and 39 Noncoding Rna (Ncrna) Sequencesmentioning

confidence: 99%

Section: Polyadenylation Signals and 39 Noncoding Rna (Ncrna) Sequencesmentioning

confidence: 99%

Section: Polyadenylation Signals and 39 Noncoding Rna (Ncrna) Sequencesmentioning

confidence: 99%

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Ending the message: poly(A) signals then and now

Proudfoot¹

2011

Genes Dev.

501

477

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“…39-End processing is an essential step in the maturation of all mRNAs and is coupled to transcription and splicing, as well as termination (Hirose and Manley 2000;Proudfoot et al 2002;Buratowski 2005). The mammalian pre-mRNA 39-end processing machinery contains more than 14 proteins giving rise to a 1-MDa complex (for review, see Colgan and Manley 1997;Zhao et al 1999;Mandel et al 2008; see also Shi et al 2009). …”

Section: -End Processing Machinerymentioning

confidence: 99%

Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

284

325

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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.

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“…The assembly of the cleavage/polyadenylation machinery requires specific signal sequences in the mRNA precursor as well as interactions of a large number of protein factors (reviewed by Mandel et al, 2008). It has been shown that the regulation of mRNA 3 0 end formation can have significant roles in cancer (Kleiman and Manley, 2001;Topalian et al, 2001;Scorilas, 2002;Rozenblatt-Rosen et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

p53 inhibits mRNA 3′ processing through its interaction with the CstF/BARD1 complex

et al. 2011

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The mechanisms involved in the p53-dependent control of gene expression following DNA damage have not been completely elucidated. Here, we show that the p53 C terminus associates with factors that are required for the ultraviolet (UV)-induced inhibition of the mRNA 3 0 cleavage step of the polyadenylation reaction, such as the tumor suppressor BARD1 and the 3 0 processing factor cleavage-stimulation factor 1 (CstF1). We found that p53 can coexist in complexes with CstF and BARD1 in extracts of UV-treated cells, suggesting a role for p53 in mRNA 3 0 cleavage following DNA damage. Consistent with this, we found that p53 inhibits 3 0 cleavage in vitro and that there is a reverse correlation between the levels of p53 expression and the levels of mRNA 3 0 cleavage under different cellular conditions. Supporting these results, a tumor-associated mutation in p53 not only decreases the interaction with BARD1 and CstF, but also decreases the UV-induced inhibition of 3 0 processing, all of which is restored by wild-type-p53 expression. We also found that p53 expression levels affect the polyadenylation levels of housekeeping genes, but not of p21 and c-fos genes, which are involved in the DNA damage response (DDR). Here, we identify a novel 3 0 RNA processing inhibitory function of p53, adding a new level of complexity to the DDR by linking RNA processing to the p53 network.

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Protein factors in pre-mRNA 3′-end processing

Cited by 351 publications

References 233 publications

Ending the message: poly(A) signals then and now

Ending the message: poly(A) signals then and now

Transcription termination by nuclear RNA polymerases

p53 inhibits mRNA 3′ processing through its interaction with the CstF/BARD1 complex

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