We have purified the yeast U5 and U6 pre-mRNA splicing small nuclear ribonucleoproteins (snRNPs) by affinity chromatography and analyzed the associated polypeptides by mass spectrometry. The yeast U5 snRNP is composed of the two variants of U5 snRNA, six U5-specific proteins and the 7 proteins of the canonical Sm core. The U6 snRNP is composed of the U6 snRNA, Prp24, and the 7 Sm-Like (LSM) proteins. Surprisingly, the yeast DEAD-box helicase-like protein Prp28 is stably associated with the U5 snRNP, yet is absent from the purified U4/U6.U5 snRNR A novel yeast U5 and four novel yeast U4/U6.U5 snRNP polypeptides were characterized by genetic and biochemical means to demonstrate their involvement in the pre-mRNA splicing reaction. We also show that, unlike the human tri-snRNP, the yeast tri-snRNP dissociated upon addition of ATP or dATP. ...
A complex composed of RNA of the small nuclear RNA (snRNA) class and protein, found in the nucleus of a eukaryotic cell. These are typically named after the snRNA(s) they contain, e.g. U1 snRNP or U4/U6 snRNP. Many, but not all, of these complexes are involved in splicing of nuclear mRNAs. [GOC:krc, GOC:mah, ISBN:0879695897]
Spinal muscular atrophy (SMA) is an often fatal neuromuscular disease that has been directly linked to the protein product of the Survival of Motor Neurons (SMN) gene. The SMN protein is tightly associated with a novel protein, SIP1, and together they form a complex with several spliceosomal snRNP p …
Plays role in pre-mRNA splicing as core component of the SMN-Sm complex that mediates spliceosomal snRNP assembly and as component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3-end processing (PubMed:19470752).
Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (PubMed:21081503, PubMed:18984161). Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also indirectly participate in cellular volume control by activation
The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by ...
Background: While genetic knockdown of RAS in mouse tumor models has substantiated it as a therapeutic target, there is no effective means of targeting RAS currently available in the clinic today. Numerous RNA interference-based studies targeting RAS have demonstrated therapeutic effects, however, effective delivery has been a major obstacle that has impeded this approach.. U1 Adaptors are a novel technology for oligonucleotide-mediated gene silencing that act by selectively interfering with polyadenylation of messenger RNA (mRNA) inside the cell nucleus. Polyadenosine (PolyA) tail addition is an obligatory step in mRNA maturation and function, and its failure results in rapid degradation of the nascent message by endogenous nucleases. The eukaryotic U1 small nuclear ribonucleoprotein complex (U1 snRNP) is best known for its role as a pre-mRNA splicing factor, but also acts naturally to silence some genes by suppressing polyadenylation.. U1 Adaptors are synthetic oligonucleotides that enable the ...
Pre-mRNA splicing takes place in an RNA machine known as the spliceosome, which consists of small nuclear ribonucleoprotein particles (snRNPs)1 and non-snRNP protein factors. The RNA components in the spliceosome form the catalytic core through a series of dynamic RNA-RNA interactions which are likely to be mediated and/or stabilized by non-snRNP protein factors (for recent reviews see Nilsen, 1998; Staley and Guthrie, 1998). Among the best characterized non-snRNP splicing factors are SR proteins which contain one or two RNA recognition motifs and a signature RS domain containing multiple serine and arginine repeats (for reviews see Fu, 1995; Manley and Tacke, 1996). The RNA recognition motifs bind to RNA sequences in a coordinated fashion to determine splicing specificity (Chandler et al., 1997) and commit pre-mRNA substrates to the splicing pathway (Fu, 1993), whereas the RS domains mediate specific protein- protein interactions in a number of spliceosomal assembly steps (Wu and Maniatis, ...
In this work, factors that affect the localization of the Lsm7 and Lsm8 proteins were investigated in order to try to understand what determines the nuclear localization of the Lsm2-8p complex. The results show that Lsm8p is a determinant for the nuclear accumulation of Lsm7p, although they do not clearly distinguish between nuclear import and nuclear retention. However, considering the effect of the nup49-313 nuclear-pore mutation as well the previously demonstrated dependence of Lsm8p nuclear accumulation on importin β (Spiller et al., 2007), Lsm8p might function as a nuclear-import determinant for the rest of the Lsm2-8p complex. The deletion studies show that most of the Lsm8p sequence seems to be essential, including the N-terminus, the Sm domain and the C-terminus. In particular, a deletion of part of the Sm domain caused a dramatic mislocalization of Lsm8p, strongly suggesting the importance of interaction with other Lsm proteins for nuclear accumulation of Lsm8p. Unexpectedly, a ...
Species, Publications, Scientific Experts, Research Grants, Research Topics, Genomes and Genes about u1 small nuclear ribonucleoprotein
Sera from some patients with systemic lupus erythematosus and other autoimmune diseases have antibodies against nuclear antigens. An example is anti-Sm sera, which recognize proteins associated with small nuclear RNA molecules [small nuclear ribonucleoprotein (snRNP) particles]. In this paper anti-Sm sera were used to probe immunoblots of various rat tissues. A previously unidentified Mr 28,000 polypeptide was recognized by these anti-Sm sera. This polypeptide, referred to as "N," is expressed in a tissue-specific manner, being most abundant in rat brain, less so in heart, and undetectable in the other tissues examined. Immunoprecipitation experiments using antibodies directed against the cap structure of small nuclear RNAs have demonstrated that N is a snRNP-associated polypeptide. Anti-Sm serum was also used to isolate a partial cDNA clone (lambda rb91) from a rat brain phage lambda gt11 cDNA expression library. On RNA blots, the 450-base-pair cDNA insert of this clone hybridized to a ...
YAOZHE; Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA (By similarity). Essential for embryogenesis. Plays a critical role in embryo sac development and gametic cell fate. Required for the correct positioning of the first division plane of zygote. May function during early embryogenesis (PubMed-20699009) (504 aa ...
This gene encodes subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the introns branch site in a sequence independent manner and may anchor the U2 snRNP to the pre-mRNA. Splicing factor 3b is also a component of the minor U12-type spliceosome. The carboxy-terminal two-thirds of subunit 1 have 22 non-identical, tandem HEAT repeats that form rod-like, helical structures. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008 ...
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View mouse Snrnp200 Chr2:127208386-127240451 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
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As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Watkins, N. J.; Segault, V.; Carpentier, B.; Nottrott, S.; Fabrizio, P.; Bachi, A.; Wilm, M.; Rosbash, M.; Branlant, C.; Luehrmann, R.: A common core RNP structure shared between the small nuclear box C/D RNPs and the spliceosomal U 4 snRNP. Cell 103, pp. 457 - 466 (2000 ...
Kit Component:- KN205120G1, SNRPB2 gRNA vector 1 in pCas-Guide vector- KN205120G2, SNRPB2 gRNA vector 2 in pCas-Guide vector- KN205120D, donor vector…
snRNP70 also known as U1 small nuclear ribonucleoprotein 70 kDa is a protein that in humans is encoded by the SNRNP70 gene. snRNP70 is a small nuclear ribonucleoprotein that associates with U1 spliceosomal RNA, forming part of the spliceosome. snRNP70 has been shown to interact with ASF/SF2, SRPK1, and ZRANB2. Antibodies towards snRNP70 are associated with mixed connective tissue disease. GRCh38: Ensembl release 89: ENSG00000104852 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000063511 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Spritz RA, Strunk K, Surowy CS, Hoch SO, Barton DE, Francke U (December 1987). "The human U1-70K snRNP protein: cDNA cloning, chromosomal localization, expression, alternative splicing and RNA-binding". Nucleic Acids Res. 15 (24): 10373-91. doi:10.1093/nar/15.24.10373. PMC 339950 . PMID 2447561. "Entrez Gene: SNRP70 small nuclear ribonucleoprotein 70kDa polypeptide (RNP antigen)". Spritz RA, Strunk K, Surowy CS, Mohrenweiser HW ...
The splicing of pre‐mRNA in the nucleus is catalyzed by a large ribonucleoprotein complex, the spliceosome (for reviews see Krämer, 1996; Burge et al., 1999). The spliceosome consists of the pre‐mRNA substrate and several small nuclear ribonucleoproteins (snRNPs), along with splicing factors not integrated into snRNPs. Each snRNP is a stable complex of a single RNA molecule (snRNA) and several proteins; some of these proteins are common to all snRNPs (the Sm proteins), while others are specific to a given snRNP (Will and Lührmann, 2001). The individual snRNPs interact during the splicing cycle in a highly dynamic manner. For example, at the start of the splicing cycle the U4 and U6 snRNPs are tightly associated by extensive RNA-RNA base‐pairing, forming a single particle termed U4/U6. This complex associates in turn with U5 snRNP to yield the U4/U6·U5 tri‐snRNP. The latter undergoes further rearrangements during the assembly of the catalytically active spliceosome. These include the ...
Small nuclear ribonucleoprotein-associated protein B and B is a protein that in humans is encoded by the SNRPB gene. The protein encoded by this gene is one of several nuclear proteins that are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the encoded protein may also play a role in pre-mRNA splicing or snRNP structure. Autoantibodies from patients with systemic lupus erythematosus frequently recognize epitopes on the encoded protein. Two transcript variants encoding different isoforms (B and B) have been found for this gene.
Small nuclear ribonucleic acid (snRNA), also commonly referred to as U-RNA, is a class of small RNA molecules that are found within the splicing speckles and Cajal bodies of the cell nucleus in eukaryotic cells. The length of an average snRNA is approximately 150 nucleotides. They are transcribed by either RNA polymerase II or RNA polymerase III. Their primary function is in the processing of pre-messenger RNA (hnRNA) in the nucleus. They have also been shown to aid in the regulation of transcription factors (7SK RNA) or RNA polymerase II (B2 RNA), and maintaining the telomeres. snRNA are always associated with a set of specific proteins, and the complexes are referred to as small nuclear ribonucleoproteins (snRNP, often pronounced "snurps"). Each snRNP particle is composed of a snRNA component and several snRNP-specific proteins (including Sm proteins, a family of nuclear proteins). The most common snRNA components of these complexes are known, respectively, as: U1 spliceosomal RNA, U2 ...
Cajal bodies (CBs) are subnuclear domains that participate in spliceosomal small nuclear ribonucleoprotein (snRNP) biogenesis and play a part in the assembly of the spliceosomal complex. The CB marker
As is known to all, p68 is a prototypic multifunctional protein, and the most well recognized function of p68 is to bind both double- and single-stranded RNA and provide energy to perform bidirectional RNA duplex unwinding activity as an ATPase [21]. Another important function of p68 is for efficient spliceosome assembling and RNA splicing [22]. Previous investigations demonstrated that p68 could unwind and separate the connection between the U1 small nuclear ribonucleoprotein particle and the [15] splice site, facilitating the dynamic formation from pre-spliceosome to spliceosome [23]. However, the assembly of the spliceosome is in an RNA helicase-independent manner [24]. RNA helicase p68 could also manifest conformational change activity enhancing the U1-5ss interaction [25]. Based on the observation, the p68 is important for RNA maturation. In succession, alternative splicing can also be regulated in this way [26].. MicroRNAs(miRNAs) are small non-coding RNAs that can affect cell development ...
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Many RNA-associated proteins contain a ribonucleoprotein (RNP) consensus octamer encompassed by a conserved 80 amino acid sequence, termed an RNA recognition motif (RRM). RRM family members contain either one (class I) or multiple (class II) copies of this motif. A class II component of the U1 small nuclear RNP (snRNP), the A protein of U1 snRNP (U1snRNP-A), contains two RRMs (RRM1 and -2), yet has only one binding domain (RRM1) that interacts specifically with stem-loop II of U1 RNA. Quantitative analysis of binding affinities of fragments of U1snRNP-A demonstrates that an 86-amino acid polypeptide is competent to bind to U1 RNA with an affinity comparable to that of the full-length protein (Kd approximately 80 nM). The carboxyl-terminal RRM2 of U1snRNP-A does not bind to U1 RNA and may recognize an unidentified heterologous RNA. It is proposed that class II proteins may function as bridges between RNA components of RNP complexes, such as the spliceosome (Lutz-Freyermuth, 1990). The RNP domain ...
In addition to finding most of the known EJC factors splicing containing variable 5 exon (v5 meoitic and mitotic paragene T codon B cell) and correlates scaffold hnRPN-I/U, with SRM160 is the more important component of the complex; it has multiple R, S, and P residues. The acinus L, S, and S-prime cDNAs contain open reading frames (ORF) read anticlockwse-L, and clockwise-R to an abundance of unspecific YWHAG from HPRD-[§§], overexpressed amino acid residues near the exon-exon junctions of mRNAs. While a stable association of development and differentiation and ACN1 condensation such as polymerase eta ribonucleoprotein U scaffold attachment after irradiation with UVC light but another protein inhibitor is replication-independent damage accumulation of residues is not necessary for UV-induced polymerase eta focus formation. Where as RNA binding protein S1, intronless [wild type] versions of SRm160 is normally also dependent on U1-2 (igG) certain non-T/non-B-ALL, cells. Small nuclear RNPs an ...
Expression of MEPCE (BCDIN3, FLJ20257, MePCE) in esophagus tissue. Antibody staining with HPA051587 and CAB026384 in immunohistochemistry.
Pre-mRNA splicing or the removal of introns from precursor messenger RNAs depends on the accurate recognition of intron sequences by the plant splicing machinery. The major components of this machinery are small nuclear ribonucleoprotein protein particles (snRNPs) which consist of snRNAs and snRNP proteins. We have analysed various aspects of intron sequence and structure in relation to splice site selection and splicing efficiency and we have cloned snRNA genes and a gene encoding the snRNP protein, U2B". In the absence of an in vitro splicing system for plants, transient expression in protoplasts and stable plant transform ations have been used to analyse splicing of intron constructs. We aim to address the function of the UsnRNP-specific protein, U2B", via the production of transgenic plants expressing antisense U2B" transcripts and epitope-tagged U2B" protein. In addition, we have cloned genes encoding other proteins which potentially interact with RNA, such as RNA helicases, and strategies ...
SNRPN - SNRPN (untagged)-Human small nuclear ribonucleoprotein polypeptide N (SNRPN), transcript variant 1 available for purchase from OriGene - Your Gene Company.
Complete information for SNRNP40 gene (Protein Coding), Small Nuclear Ribonucleoprotein U5 Subunit 40, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for SNRNP27 gene (Protein Coding), Small Nuclear Ribonucleoprotein U4/U6.U5 Subunit 27, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
In eukaryotic cells, the Sm-proteins B/B, D1, D2, D3, E, F, and G form a heteroheptameric protein core shared between all uracil-rich small nuclear ribonucleoprotein (U-snRNP) complexes. Like native SmD1, DIARECT™s recombinant SmD1 contains symmetrically dimethylated arginine residues. DIARECT™ antigens are for further manufacturing or research use only. ...
Small ribonucleoproteins (RNPs) are essential components of all cells. Eukaryotic gene expression requires a constellation of small non-coding RNP particles tha...
PRP31_HUMAN RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp31; AltName: Full=Pre-mRNA-processing factor 31; AltName: Full=Serologically defined breast cancer antigen NY-BR-99; AltName: Full=U4/U6 snRNP 61 kDa protein; Short=Protein 61K; Short=hPrp31 ...
Despite "decades of persistent failure to create life by the spark in the soup method,"1 evolutionary biochemists are still trying to find an exclusively naturalistic explanation for how the first cell developed. Many possible chemical precursors to life have been systematically ruled out by rigorous experiments. What they have found is that the molecules necessary for life are found exclusively within cells that are already living.. One explanation proposed by evolutionists was the "RNA world" hypothesis, which holds that the first molecules to have spontaneously materialized in an ancient chemical soup were RNAs.2 This has met with too many obstacles to remain viable, so an embellishment to the RNA world was recently proposed by Thomas Cech in the journal Cell.3 He suggested that the first molecules to evolve toward life were ribonucleoproteins (RNPs), molecules made partly of RNA and partly of protein.. In nature, RNPs are found only inside cells. They have specific shapes, sizes, and ...
We have shown that Dart5-mediated methylation of Sm proteins is not essential for snRNP biogenesis. The results uncover a novel role for dart5 in specification of the germline and in spermatocyte maturation. Because disruption of both dart5 and valois causes the specific loss of sDMA-modified Sm pro …
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The current model of spliceosome assembly was developed principally from the in vitro pattern of small nuclear ribonucleoprotein (snRNP) particle association with synthetic splicing substrates (reviewed in Moore et al., 1993; Madhani and Guthrie, 1994; Krämer, 1996). In mammals and yeast, spliceosome assembly progresses by the sequential addition of the U1 snRNP→U2 snRNP→U4/U6.U5 tri‐snRNP particles to the pre‐mRNA. Before 5′ splice‐site cleavage (chemical step I in splicing), the affinities of the U1 and U4 snRNAs for the splicing complex are greatly reduced and, under many (Pikielny et al., 1986; Cheng and Abelson, 1987; Konarska and Sharp, 1987) although not all (Blencowe et al., 1989) isolation conditions, the U4 snRNA is lost from the spliceosome. This model of spliceosome assembly is supported by the abridged spliceosome assembly profiles observed when splicing is inhibited by specific mutations in the pre‐mRNA or when one of the many trans‐acting components of splicing is ...
|p|Dyskeratosis congenita 1, dyskerin,is a member of the H/ACA snoRNPs (small nucleolar ribonucleoproteins). The H/ACA snoRNPs also include the NOLA1, 2 and 3 proteins. The protein encoded by this gene and the three NOLA proteins localize to the dense fibrillar components of nucleoli and to coiled (Cajal) bodies in the nucleus. Both 18S rRNA production and rRNA pseudouridylation are impaired if any one of the four proteins is depleted. The protein encoded by this gene is related to the Saccharomyces cerevisiae Cbf5p and Drosophila melanogaster Nop60B proteins. The gene lies in a tail-to-tail orientation with the palmitoylated erythrocyte membrane protein (MPP1) gene and is transcribed in a telomere to centromere direction. Both nucleotide substitutions and single trinucleotide repeat polymorphisms have been found in this gene.|/p|
Intracellular TLRs have limited ability to discriminate host versus foreign nucleic acids (Haas et al., 2008). Several host factors, including anti-DNA antibodies, antimicrobial peptide LL37, or the nuclear DNA-binding protein HMGB1, alone or in combination, facilitate entry of self-DNA into the endosomes of pDCs, where they trigger TLR9 to induce type 1 IFN responses (Lande et al., 2007; Marshak-Rothstein and Rifkin, 2007; Tian et al., 2007). Similarly, autoantibody-self small nuclear ribonucleoprotein complexes can activate TLR7 through FcγRII to induce IFN (Vollmer et al., 2005; Savarese et al., 2006). This might lead to the constitutive activation of pDCs, which contributes to the autoimmune pathology of systemic lupus erythematosus and psoriasis. It will be of further interest to study if the BST2-ILT7-mediated controlling mechanism is breached in patients with systemic lupus erythematosus and psoriasis (Blanco et al., 2001; Lande et al., 2007; Marshak-Rothstein and Rifkin, 2007), which ...
The 5 and 3 domains of yeast U6 snRNA contain sequences that are thought to be important for binding to Prp24 and Lsm proteins. By extensive mutational analysis of yeast U6 snRNA, we confirmed that the 3 terminal uridine tract of U6 snRNA is important for U6 binding to Lsm proteins in yeast. Binding of Prp24 protein to U6 RNA is dependent on or is strongly enhanced by U6 binding of Lsm proteins. This supports a model for U6 snRNP assembly in which U6 RNA binds to the Lsm2-8 core prior to binding Prp24 protein. Using compensatory base-pairing analysis, we show that at least half of the recently identified U6 telestem as well as a nucleotide sequence in the other half of the telestem are important for binding of U6 RNA to Prp24 protein. Surprisingly, disruption of base pairing in the unconfirmed half of the telestem enhanced U6-Prp24 binding. Truncation of the entire 3 terminal domain or nearly the entire 5 terminal domain of yeast U6 allowed for detectable levels of splicing to proceed in ...
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RNA-Protein Complexes: Roles in Gene Expression Noncoding RNAs are important for every step of gene expression. We concentrate on nuclear noncoding RNAs complexed with proteins, where the most famous small nuclear RNPs (snRNPs) participate in pre-mRNA splicing. Current efforts are aimed at understanding how splicing influences downstream events in gene expression via the exon junction complex (EJC), how microRNA biogenesis is regulated during the nuclear maturation steps, and what is the mechanism and function of readthrough transcripts that arise from ~10% of human genes when cells are exposed to stress (osmotic, heat shock or oxidative). Some primate herpesviruses [Epstein-Barr virus (EBV), Herpesvirus saimiri (HVS), and Kaposi sarcoma virus (KSHV)] produce noncoding RNAs that associate with host cell proteins to form snRNPs. Recent investigations have uncovered an unexpected function for an abundant EBV snRNP in the production of viral particles - which is essential for oncogenesis, have ...