The human immunodeficiency virus type 1 polyadenylylation signal: a 3' long terminal repeat element upstream of the AAUAAA necessary for efficient polyadenylylation.

Valsamakis, Alexandra; Zeichner, Steven L.; Carswell, Susan; Alwine, James C.

doi:10.1073/pnas.88.6.2108

Cited by 128 publications

(115 citation statements)

References 29 publications

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“…In addition to the AAUAAA motif and the downstream GU-rich or U-rich element of mammalian systems, upstream sequences that contribute to the efficiency of mRNA 3Ј end formation were also identified in the mammalian viruses simian virus 40 (6,36), adenovirus (8,9), hepatitis B virus (29), and human immunodeficiency virus type 1 (3,11,12,38,39). These elements function in an orientation-and position-dependent manner, and several appear to be functionally analogous.…”

Section: Discussionmentioning

confidence: 99%

3′-end-forming signals of yeast mRNA

Guo

Sherman²

1996

Trends in Biochemical Sciences

151

126

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Section: Discussionmentioning

confidence: 99%

3′-end-forming signals of yeast mRNA

Guo

Sherman²

1996

Trends in Biochemical Sciences

151

126

View full text Add to dashboard Cite

“…In particular, the GUrich sequence (or downstream sequence element, DSE) present just past the mRNA 39 end in the immediate gene 39 flanking region was shown to enhance 39-end formation Proudfoot 1984, 1987;McLauchlan et al 1985). Similarly, the sequence immediately upstream of AAUAAA (upstream sequence element, USE) (Carswell and Alwine 1989;DeZazzo et al 1991;Valsamakis et al 1991;Moreira et al 1995;Brackenridge and Proudfoot 2000;Venkataraman et al 2005;Danckwardt et al 2007) can in some cases act as an enhancing element for 39-end processing efficiency. Finally, the actual nucleotides at the site of 39-end cleavage can also influence the efficiency of this process (Chen et al 1995).…”

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

confidence: 99%

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

Proudfoot¹

2011

Genes Dev.

505

486

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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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“…This is supported by the observation that the 64-kD subunit of CstF interacts with the DSE (MacDonald et al 1994~ Y. Takagaki and J. Manley, in prep. ) Valsamakis et al 1991, 1992~ Gilmartin et al 1992~ Schek et al 1992. Previously, we have described the USE motifs found in SV40 late mRNA Alwine 1989~ Schek et al 1992} and have shown that the UIA protein utilizes these motifs to interact with the RNA (Lutz and Alwine 1994).…”

mentioning

confidence: 99%

Interaction between the U1 snRNP-A protein and the 160-kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation efficiency in vitro.

Lutz¹,

Murthy²,

Schek³

et al. 1996

Genes Dev.

Self Cite

154

131

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We have previously shown that the U1 snRNP-A protein {U1A) interacts with elements in the SV40 late polyadenylation signal and that this association increases polyadenylation efficiency. It was postulated that this interaction occurs to facilitate protein-protein association between components of the U1 snRNP and proteins of the polyadenylation complex. We have now used GST fusion protein experiments, coimmunoprecipitations and Far Western blot analyses to demonstrate direct binding between U1A and the 160-kD subunit of cleavage--polyadenylation specificity factor (CPSF}. In addition, Western blot analyses of fractions from various stages of CPSF purification indicated that U1A copurified with CPSF to a point but could be separated in the highly purified fractions. These data suggest that UIA protein is not an integral component of CPSF but may be able to interact and affect its activity. In this regard, the addition of purified, recombinant U1A to polyadenylation reactions containing CPSF, polyIA) polymerase, and a precleaved RNA substrate resulted in concentration-dependent increases in both the level of polyadenylation and polylA} tail length. In agreement with the increase in polyadenylation efficiency caused by U1A, recombinant U1A stabilized the interaction of CPSF with the AAUAAA-containing substrate RNA in electrophoretic mobility shift experiments. These findings suggest that, in addition to its function in splicing, U1A plays a more global role in RNA processing through effects on polyadenylation.[ Moore et al. 1993; Sachs and Wahle 1993}. Splicing involves removal of intronic sequences and ligation of exons by a complex set of small nuclear ribonucleoprotein particles (snRNPsl and other factors known collectively as the spliceosome. Polyadenylation is the process by which the 3' end is formed through specific endonucleolytic cleavage of the precursor RNA and the addition of -250 adenosine residues. Both in vitro (Niwa et al. 1990;Berget 1991} and in vivo (Chiou et al. 1991;Nesic et al. 1993; Nesic and Maquat 1994} experiments 4These authors contributed equally to this work. SCorresponding author.have suggested that the processes of splicing and polyadenylation might be functionally linked. This proposal has been supported by our previous report that the U1 snRNP-A protein (U1A) interacts with elements in the SV40 late polyadenylation signal and that these interactions increase polyadenylation efficiency (Lutz and A1-wine 1994}. These data support the exon definition model of Berget and co-workers (for review, see Berget 1995}, which suggests that components of both the spliceosome and the polyadenylation complex may interact to define the last exon and affect the efficiencies of polyadenylation and last intron removal.There are currently five established mammalian factors comprising the complex that cleaves and polyadenylates substrate RNAs: cleavage-polyadenylation specificity factor (CPSF), cleavage stimulatory factor (CstF), polYIA) polymerase {PAP}, and cleavage factors I and II (CFI and CFII}...

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The human immunodeficiency virus type 1 polyadenylylation signal: a 3' long terminal repeat element upstream of the AAUAAA necessary for efficient polyadenylylation.

Abstract: ABSTRACT

Cited by 128 publications

References 29 publications

3′-end-forming signals of yeast mRNA

3′-end-forming signals of yeast mRNA

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

Interaction between the U1 snRNP-A protein and the 160-kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation efficiency in vitro.

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