Modulation of alternative splicing of adenoviral E1A transcripts: factors involved in the early-to-late transition.

Gattoni, Renata; Chébli, Karim; Himmelspach, Michèle; Stévenin, James

doi:10.1101/gad.5.10.1847

Cited by 25 publications

(25 citation statements)

References 56 publications

(57 reference statements)

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“…The 11S and 10S mRNAs accumulate late during infection and have been observed in vitro (31)(32)(33). The 9S mRNA becomes most abundant at late times ofviral infection (34)(35)(36) and the switch toward 9S mRNA production can be reproduced in vitro by reducing the ionic strength (37) or by addition of late viral transcripts, which act by sequestering splicing factors (38). The splicing factor SF2/ASF promotes proximal 13S and 12S 5'SS utilization in vitro (16,39 (Fig.…”

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confidence: 87%

“…To demonstrate that high levels ofAl mRNA in transfected cells were not responsible for the shift in EMA 5'SS selection by sequestering regulatory splicing factors (38), transfections were performed with an Al cDNA containing a frameshift mutation at codon 23 in the hnRNP Al coding sequences. The level ofAl transcripts generated from this mutated Al cDNA (Alfs) was equivalent to the level produced with the wild-type Al cDNA (Fig.…”

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confidence: 99%

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The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5' splice site selection in vivo.

Yang

Bani

et al. 1994

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

180

158

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(2,3) and depletion of hnRNP C proteins from HeLa extracts reduces splicing activity (2). At least four hnRNP proteins (Al, C, D, and I/PTB) can bind to the polypyrimidine stretch found at the 3' splice site (3'SS) of introns (4-9). hnRNP I/PTB has also been found associated with various 5' splice site (5'SS) sequences (10) and binding to a specific intron region appears to negatively regulate exon inclusion (8). The transient association of hnRNP proteins with premRNA suggests that these proteins modulate the interaction of splicing factors (4, 11). tTo whom reprint requests should be addressed. 6924The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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confidence: 87%

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confidence: 99%

The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5' splice site selection in vivo.

Yang

Bani

et al. 1994

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

180

158

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“…Alternative splicing of the E1A pre-mRNA generates three major isoforms (13S, 12S, and 9S) and two minor isoforms (11S and 10S) ( Figure 7A) (Caceres et al, 1994). Several proteins, among which are hnRNP A1, SF2/ASF, 9G8, and SC35, have been shown to modulate the production of these isoforms by altering 5Ј splice-site selection (Gattoni et al, 1991;Caceres et al, 1994). We have shown that the recruitment of HAP, and other RNA processing factors, to stressinduced SNBs peaks at 3 h of recovery from heat shock, and an additional 3 h is required before the distribution of the protein becomes again comparable with that observed in unstressed cells (Weighardt et al, 1999).…”

Section: Stress Treatments Affect Alternative Splicing Program Of E1amentioning

confidence: 99%

Stress-induced Nuclear Bodies Are Sites of Accumulation of Pre-mRNA Processing Factors

Denegri

Chiodi

Corioni

et al. 2001

MBoC

155

143

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Heterogeneous nuclear ribonucleoprotein (hnRNP) HAP (hnRNP A1 interacting protein) is a multifunctional protein with roles in RNA metabolism, transcription, and nuclear structure. After stress treatments, HAP is recruited to a small number of nuclear bodies, usually adjacent to the nucleoli, which consist of clusters of perichromatin granules and are depots of transcripts synthesized before stress. In this article we show that HAP bodies are sites of accumulation for a subset of RNA processing factors and are related to Sam68 nuclear bodies (SNBs) detectable in unstressed cells. Indeed, HAP and Sam68 are both present in SNBs and in HAP bodies, that we rename "stress-induced SNBs." The determinants required for the redistribution of HAP lie between residue 580 and 788. Different portions of this region direct the recruitment of the green fluorescent protein to stress-induced SNBs, suggesting an interaction of HAP with different components of the bodies. With the use of the 580 -725 region as bait in a two-hybrid screening, we have selected SRp30c and 9G8, two members of the SR family of splicing factors. Splicing factors are differentially affected by heat shock: SRp30c and SF2/ASF are efficiently recruited to stress-induced SNBs, whereas the distribution of SC35 is not perturbed. We propose that the differential sequestration of splicing factors could affect processing of specific transcripts. Accordingly, the formation of stress-induced SNBs is accompanied by a change in the splicing pattern of the adenovirus E1A transcripts.

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“…Other SR proteins, e.g., SRp20, 9G8, SRp55, and SRp75, promote 12S splicing (18,37,48). The early to late shift from 13S to 9S mRNA splicing has been proposed to be triggered by a titration of functionally active SR proteins by high-molecularweight adenovirus major late transcript, produced late after infection (13,18,25).…”

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Overexpression of Essential Splicing Factor ASF/SF2 Blocks the Temporal Shift in Adenovirus Pre-mRNA Splicing and Reduces Virus Progeny Formation

Molin

Akusjärvi

2000

J Virol

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Expression of cytoplasmic mRNA from most adenovirus transcription units is subjected to a temporal regulation at the level of alternative pre-mRNA splicing. The general tendency is that splice site selection changes from proximal to distal late after infection. Interestingly, ASF/SF2, which is a prototypical member of the SR family of splicing factors, has the opposite effect on splice site selection, inducing an increase in proximal splice site usage. We have previously shown that SR proteins late during an adenovirus infection become partially inactivated as splicing regulatory proteins. A prediction from these results is that overexpression of an SR protein, such as ASF/SF2, during virus growth will interfere with virus replication by disturbing the balance of functional and nonfunctional ASF/SF2 in the infected cell. To test this hypothesis, we reconstructed a recombinant adenovirus expressing ASF/SF2 under the transcriptional control of a regulated promoter. The results show that, as predicted, induction of ASF/SF2 during lytic virus growth prevents the early to late shift in mRNA expression from both early (E1A and E1B) and late (L1) transcription units. Furthermore, ASF/SF2 overexpression blocks viral DNA replication and reduces selectively cytoplasmic accumulation of major late mRNA, resulting in a lower virus yield. Collectively, our results provide additional support for the hypothesis that viral control of SR protein function is important for the proper expression of viral proteins during lytic virus growth.Adenovirus gene expression is to a large extent regulated at the level of pre-mRNA alternative splicing (reviewed in reference 21). Thus, the majority of adenovirus transcription units produce multiple differently spliced cytoplasmic mRNAs. The production of several mRNAs from each viral transcription unit increases the coding potential of the viral genome and, furthermore, enables the virus to control viral gene expression by regulating the specificity of RNA splicing. Importantly, the accumulation of alternatively spliced mRNAs is subjected to a temporal regulation, with distinct mRNA species accumulating at different time points of infection (reviewed in reference 21).Although the mechanism(s) responsible for this shift in RNA splice site choice is far from clear, a number of studies have suggested that the cellular SR family of splicing factors plays a critical role in this regulation. SR proteins constitute a family of splicing factors that are essential for generic premRNA splicing (reviewed in references 12 and 28). They contain one or two amino-terminal RNA binding domains and a characteristic carboxy-terminal RS domain consisting of repeats of serine/arginine dipeptides of variable length, hence the name SR proteins. The RNA recognition motif determines the RNA binding specificity, whereas the RS domain functions as an effector domain mediating interaction with other splicing factors (reviewed in references 12 and 28). SR proteins participate at multiple steps during the initial stages of ...

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Modulation of alternative splicing of adenoviral E1A transcripts: factors involved in the early-to-late transition.

Cited by 25 publications

References 56 publications

The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5' splice site selection in vivo.

The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5' splice site selection in vivo.

Stress-induced Nuclear Bodies Are Sites of Accumulation of Pre-mRNA Processing Factors

Overexpression of Essential Splicing Factor ASF/SF2 Blocks the Temporal Shift in Adenovirus Pre-mRNA Splicing and Reduces Virus Progeny Formation

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