The Splicing Factor PSF is Part of a Large Complex That Assembles in the Absence of pre-mRNA and Contains All 5 snRNPs

Peng, Rui; Hawkins, Ian C.; Link, Andrew J.; Patton, James G.

doi:10.4161/rna.3.2.3017

Cited by 25 publications

(31 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…SFPQ and NONO are known members of the spliceosome and have previously been identified in a large scale antibody- Arginine methylation of SFPQ www.rnajournal.org 349 based proteomic analysis (Rappsilber et al 2002;Peng et al 2006). A comparison of the proteins identified in these studies with data presented here, reveals a significant corroboration (see Supplemental Table S1).…”

Section: Resultssupporting

confidence: 70%

“…The results shown in Figure 1E demonstrate that the presence of magnesium ions and ATP had negligible impact on enrichment profiles in either splicing buffer or PBS. These findings are consistent with those of Peng et al (2006) were under in vitro splicing conditions, SFPQ associates with all five splicing snRNPs as well as many other splicing factors regardless of the presence of exogenous premRNA.…”

Section: Ionic Strength Alters the Sfpq/nono Complexsupporting

confidence: 80%

“…NONO/p54nrb is homologous to the C-terminus of SFPQ/ PSF (Shav-Tal and Zipori 2002) and has been shown to associate with SFPQ/PSF (Zhang et al 1993;Straub et al 1998;Peng et al 2002;Shav-Tal and Zipori 2002;Hanna et al 2006). SFPQ and NONO have been identified in proteomic studies of the spliceosome and in splicing-related complexes (Rappsilber et al 2002;Peng et al 2006). Furthermore, in the absence of SFPQ/PSF, spliceosome formation (complexes A and B) is severely impaired (Patton et al 1993).…”

Section: Introductionmentioning

confidence: 99%

“…The enrichment of the SFPQ/NONO complex using Ni-NTA OTCs was also performed under typical splicing conditions (60 mM KCl in the presence of additional divalent cations, ATP, and phosphocreatinine) (Peng et al 2006). Under such conditions, Ni-NTA PhyCap OTC enrichments show a reduction in the yield of purified SFPQ/NONO complex (see Fig.…”

Section: Ionic Strength Alters the Sfpq/nono Complexmentioning

confidence: 99%

See 3 more Smart Citations

Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its association with mRNA

Snijders

Hautbergue

Bloom

et al. 2015

RNA

View full text Add to dashboard Cite

Splicing factor proline-and glutamine-rich (SFPQ) also commonly known as polypyrimidine tract-binding protein-associatedsplicing factor (PSF) and its binding partner non-POU domain-containing octamer-binding protein (NONO/p54nrb), are highly abundant, multifunctional nuclear proteins. However, the exact role of this complex is yet to be determined. Following purification of the endogeneous SFPQ/NONO complex, mass spectrometry analysis identified a wide range of interacting proteins, including those involved in RNA processing, RNA splicing, and transcriptional regulation, consistent with a multifunctional role for SFPQ/NONO. In addition, we have identified several sites of arginine methylation in SFPQ/PSF using mass spectrometry and found that several arginines in the N-terminal domain of SFPQ/PSF are asymmetrically dimethylated. Furthermore, we find that the protein arginine N-methyltransferase, PRMT1, catalyzes this methylation in vitro and that this is antagonized by citrullination of SFPQ. Arginine methylation and citrullination of SFPQ/PSF does not affect complex formation with NONO. However, arginine methylation was shown to increase the association with mRNA in mRNP complexes in mammalian cells. Finally we show that the biochemical properties of the endogenous complex from cell lysates are significantly influenced by the ionic strength during purification. At low ionic strength, the SFPQ/NONO complex forms large heterogeneous protein assemblies or aggregates, preventing the purification of the SFPQ/NONO complex. The ability of the SFPQ/NONO complex to form varying protein assemblies, in conjunction with the effect of post-translational modifications of SFPQ modulating mRNA binding, suggests key roles affecting mRNP dynamics within the cell.

show abstract

Section: Resultssupporting

confidence: 70%

Section: Ionic Strength Alters the Sfpq/nono Complexsupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Section: Ionic Strength Alters the Sfpq/nono Complexmentioning

confidence: 99%

See 2 more Smart Citations

Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its association with mRNA

Snijders

Hautbergue

Bloom

et al. 2015

RNA

View full text Add to dashboard Cite

show abstract

“…A c c e p t e d M a n u s c r i p t 12 SFPQ has been most carefully studied of these two proteins and it is involved in spliceosome formation and catalysis of pre-mRNA splicing [20][21][22]. However, SFPQ also has other cellular functions and in association with other protein since it has been shown to be involved in nonhomologues DNA recombination and DNA damage response [23,24].…”

Section: Discussionmentioning

confidence: 99%

Identification of genes associated to 2′,2′-difluorodeoxycytidine resistance in HeLa cells with a lentiviral short-hairpin RNA library

Karlsson

Johansson

2011

Biochemical Pharmacology

View full text Add to dashboard Cite

Please cite this article as: Xu Y, Karlsson A, Johansson M, Identification of genes associated to 2',2'-difluorodeoxycytidine resistance in HeLa cells with a lentiviral short-hairpin RNA library, Biochemical Pharmacology (2010Pharmacology ( ), doi:10.1016Pharmacology ( /j.bcp.2011 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. identified by sequence analysis. 16 cell lines with putative target genes previously not associated to dFdC resistance were identified. Chemically synthesized short-interfering RNAs (siRNAs) directed against the target genes were used to verify that the decreased expression of the identified genes caused dFdC resistance. Using these techniques we identified two splicing factor proteins, serine/arginine-rich splicing factor 3 (SRSF3) and splicing factor proline/glutamine-rich (SFPQ), that induced resistance to dFdC as well as other pyrimidine nucleoside analogs when their expression was decreased in HeLa cells.

show abstract

Dynamics of galectin-3 in the nucleus and cytoplasm

Haudek

Spronk

Voss

et al. 2010

Biochimica et Biophysica Acta (BBA) - General Subjects

145

118

View full text Add to dashboard Cite

This review summarizes selected studies on galectin-3 (Gal3) as an example of the dynamic behavior of a carbohydrate-binding protein in the cytoplasm and nucleus of cells. Within the 15-member galectin family of proteins, Gal3 (Mr ~30,000) is the sole representative of the chimera subclass in which a proline- and glycine-rich NH2-terminal domain is fused onto a COOH-terminal carbohydrate recognition domain responsible for binding galactose-containing glycoconjugates. The protein shuttles between the cytoplasm and nucleus on the basis of targeting signals that are recognized by importin(s) for nuclear localization and exportin-1 (CRM1) for nuclear export. Depending on the cell type, specific experimental conditions in vitro, or tissue location, Gal3 has been reported to be exclusively cytoplasmic, predominantly nuclear, or distributed between the two compartments. The nuclear versus cytoplasmic distribution of the protein must reflect, then, some balance between nuclear import and export, as well as mechanisms of cytoplasmic anchorage or binding to a nuclear component. Indeed, a number of ligands have been reported for Gal3 in the cytoplasm and in the nucleus. Most of the ligands appear to bind Gal3, however, through protein-protein interactions rather than through protein-carbohydrate recognition. In the cytoplasm, for example, Gal3 interacts with the apoptosis repressor Bcl-2 and this interaction may be involved in Gal3’s anti-apoptotic activity. In the nucleus, Gal3 is a required pre-mRNA splicing factor; the protein is incorporated into spliceosomes via its association with the U1 small nuclear ribonucleoprotein (snRNP) complex. Although the majority of these interactions occur via the carbohydrate recognition domain of Gal3 and saccharide ligands such as lactose can perturb some of these interactions, the significance of the protein’s carbohydrate-binding activity, per se, remains a challenge for future investigations.

show abstract

The Splicing Factor PSF is Part of a Large Complex That Assembles in the Absence of pre-mRNA and Contains All 5 snRNPs

Cited by 25 publications

References 45 publications

Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its association with mRNA

Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its association with mRNA

Identification of genes associated to 2′,2′-difluorodeoxycytidine resistance in HeLa cells with a lentiviral short-hairpin RNA library

Dynamics of galectin-3 in the nucleus and cytoplasm

Contact Info

Product

Resources

About