Identification and characterization of Prp45p and Prp46p, essential pre-mRNA splicing factors

Albers, M.; Diment, Ann; Muraru, Mariela; Russell, Caroline S.; Beggs, Jean D.

doi:10.1261/rna.2119903

Cited by 57 publications

(70 citation statements)

References 51 publications

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“…The transcriptional elongation factor TAT-SF1 forms a stable complex with the spliceosome [38] and its homologue in yeast (Cus2) has been shown to function as a critical proofreading enzyme during early spliceosome assembly [39,40], suggesting that TAT-SF1/Cus2 may be a dual function protein in transcription and mRNA splicing. Similarly, SKIP/Prp45 has been characterized as a dual functional factor in both transcriptional elongation and splicing [14,41]. These findings indicate that the transcriptional machinery is structurally and functionally intertwined with specific components of the splicing machinery.…”

Section: Multiple Molecular Contacts To Facilitate Functional Couplingmentioning

confidence: 92%

Functional integration of transcriptional and RNA processing machineries

Pandit

Wang

2008

Current Opinion in Cell Biology

153

134

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Co-transcriptional RNA processing not only permits temporal RNA processing before the completion of transcription, but also allows sequential recognition of RNA processing signals on nascent transcripts threading out from the elongating RNAPII complex. Rapid progress in recent years has established multiple contacts that physically connect the transcription and RNA processing machineries, which centers on the C-terminal domain (CTD) of the largest subunit of RNAPII. While co-transcriptional RNA processing has been substantiated, the evidence for "reciprocal" coupling starts to emerge, which emphasizes functional integration of transcription and RNA processing machineries in a mutually beneficial manner for efficient and regulated gene expression.

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Section: Multiple Molecular Contacts To Facilitate Functional Couplingmentioning

confidence: 92%

Functional integration of transcriptional and RNA processing machineries

Pandit

Wang

2008

Current Opinion in Cell Biology

153

134

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“…Ben-Yehuda et al (2000) predicted TPRs 1-9 correspond to TPRs III, V, VII, VIII, and X-XIV, respectively; Nakatsu et al (2000) predicted that TPR-containing proteins are involved in different biological pathways; and TPR motifs have been implicated in protein-protein interactions. Indeed, Ntc90 has been shown to interact with several NTC components, including Ntc85, Ntc77, Ntc31, Ntc30, and Ntc20 (Chen et al 2002), and other putative NTC components Cwc2, Prp46 , and Prp45 (Albers et al 2003). Another protein, Yju2, associated with NTC, but FIGURE 1.…”

Section: Deletion Analysis Of Ntc90mentioning

confidence: 98%

Ntc90 is required for recruiting first step factor Yju2 but not for spliceosome activation

Chang¹,

Chen²,

Cheng³

2009

RNA

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The Prp19-associated complex (NineTeen Complex [NTC]) is required for spliceosome activation by specifying interactions of U5 and U6 with pre-mRNA on the spliceosome after the release of U4. The NTC consists of at least eight protein components, including two tetratricopeptide repeat (TPR)-containing proteins, Ntc90 and Ntc77. Ntc90 has nine copies of the TPR with seven clustered in the carboxy-terminal half of the protein, and interacts with all identified NTC components except for Prp19 and Ntc25. It forms a stable complex with Ntc31, Ntc30, and Ntc20 in the absence of Ntc25, when other interactions between NTC components are disrupted. In this study, we used both biochemical and genetic methods to analyze the structure of Ntc90, and its function in maintaining the integrity of the NTC and in NTC-mediated spliceosome activation. Our results show that Ntc90 interacts with Ntc31, Ntc30, and other NTC components through different regions of the protein, and that its function may be regulated by Ntc31 and Ntc30. Ntc90 is not required for the association of Prp19, Ntc85, Ntc77, Ntc25, and Ntc20, or for their binding to the spliceosome. It is also not required for NTC-mediated spliceosome activation, but is required for the recruitment of Yju2, which is involved in the first catalytic reaction after the function of Prp2. Our results demonstrate a novel role of the NTC in recruiting splicing factors to the spliceosome after its activation.

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“…Hence, hPrp8 associates, probably indirectly, with nuclear receptor promoter regions of the vitamin D response element (Zhang et al 2003). The yeast homolog of hSKIP, yPrp45p is known to have a role in splicing (Albers et al 2003) and hSKIP was copurified with the catalytically active spliceosome and the U5/Prp19 complex . All the human spliceosomal proteins were identified, including Prp8p and the same proteins that were found at the vitamin D response element namely, U5-200K, U5-116K, and PSF.…”

Section: Human Prp8mentioning

confidence: 99%

Prp8 protein: At the heart of the spliceosome

Grainger¹,

Beggs²

2005

RNA

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322

386

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Pre-messenger RNA (pre-mRNA) splicing is a central step in gene expression. Lying between transcription and protein synthesis, pre-mRNA splicing removes sequences (introns) that would otherwise disrupt the coding potential of intron-containing transcripts. This process takes place in the nucleus, catalyzed by a large RNA-protein complex called the spliceosome. Prp8p, one of the largest and most highly conserved of nuclear proteins, occupies a central position in the catalytic core of the spliceosome, and has been implicated in several crucial molecular rearrangements that occur there. Recently, Prp8p has also come under the spotlight for its role in the inherited human disease, Retinitis Pigmentosa.Prp8 is unique, having no obvious homology to other proteins; however, using bioinformatical analysis we reveal the presence of a conserved RNA recognition motif (RRM), an MPN/JAB domain and a putative nuclear localization signal (NLS). Here, we review biochemical and genetical data, mostly related to the human and yeast proteins, that describe Prp8's central role within the spliceosome and its molecular interactions during spliceosome formation, as splicing proceeds, and in post-splicing complexes. NOTE ON NOMENCLATUREIn this review, Prp8 and Prp8p represent the protein product of the wild-type PRP8 gene of Saccharomyces cerevisiae, while prp8-1 is an example of a mutant allele of the PRP8 gene. Human Prp8 protein is designated hPrp8, also known in the literature as PRPF8, PRPC8, p220, and 220K. In some places, to avoid confusion, yPrp8 is used to distinguish the yeast (S. cerevisiae) protein from the human form. sPrp8 SPP42 (Schmidt et al. 1999) or sPrp8 cwf6 (McDonald et al. 1999;Ohi et al. 2002) defines the ortholog in Schizosaccharomyces pombe. Confusingly, the cdc28 gene in S. pombe is also referred to as prp8 as a consequence of its role in both pre-mRNA splicing and cell cycle progression, and there is also a temperature-sensitive allele called prp8-1 that causes accumulation of pre-mRNA upon a shift to nonpermissive temperatures (Lundgren et al. 1996;Imamura et al. 1998). Cdc28 prp8 encodes a 112-kDa DEAH-box protein. This protein is not the ortholog of the U5 snRNP protein of S. cerevisiae that is discussed here.In discussions of pre-mRNA-protein cross-links or mutations that affect intron-exon junctions, 5ЈSS+2 refers to the second intronic base from the 5Ј end of the intron, 5ЈSS-2 is the penultimate base of the 5Ј exon, and 3ЈSS-2 is the penultimate base of the intron. PRE-mRNA SPLICINGPre-mRNA splicing involves two trans-esterification reactions within the highly dynamic spliceosome complex. A vast amount of mainly biochemical data led to a consensus view of an ordered pathway of spliceosome assembly that will be described in outline here (for further details, see Kramer 1996;Burge et al. 1999;Brow 2002). The small nuclear RNA-protein (snRNP) complexes, known as U1, U2, U4, U5, and U6 snRNPs, play key roles. U1 is the first snRNP to associate with pre-mRNA, interacting with the 5Ј splice site (5Ј...

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Identification and characterization of Prp45p and Prp46p, essential pre-mRNA splicing factors

Cited by 57 publications

References 51 publications

Functional integration of transcriptional and RNA processing machineries

Functional integration of transcriptional and RNA processing machineries

Ntc90 is required for recruiting first step factor Yju2 but not for spliceosome activation

Prp8 protein: At the heart of the spliceosome

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