Overexpression of SbSKIP, A Pre-mRNA splicing factor from Sorghum bicolor, enhances root growth and drought tolerance in Petunia hybrida

Mild heat treatment of HeLa cell nuclear extracts (NE) selectively inhibits pre-mRNA splicing. Heat-inactivated extracts can be complemented by a small amount of untreated NE. Utilizing this complementation assay and a combination of ion-exchange, affinity, and hydrophobic chromatography, a heat reversal factor (HRF) was purified from NE that is required to rescue pre-mRNA splicing from a heat-inactivated extract. This activity in its most purified form consistently copurified in a fraction containing two 70-kDa proteins and a minor polypeptide of approximately 100 kDa. It was free of the major small nuclear RNAs, sensitive to protease, and required to rescue spliceosome formation from a heat-inactivated nuclear extract. These results suggest that this factor is a protein that may be an important component in pre-mRNA splicing, or alternatively, it may be involved in renaturation of a heat-sensitive splicing factor.

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Demonstration of a dynamic, transcription-dependent organization of pre-mRNA splicing factors in polytene nuclei.

The Journal of Cell Biology ◽

10.1083/jcb.133.5.929 ◽

1996 ◽

Vol 133 (5) ◽

pp. 929-941 ◽

Cited By ~ 26

Author(s):

G Baurén ◽

W Q Jiang ◽

K Bernholm ◽

F Gu ◽

L Wieslander

Keyword(s):

Mrna Splicing ◽

Splicing Factor ◽

Splicing Factors ◽

Chironomus Tentans ◽

Transcription Inhibition ◽

Physiological Conditions ◽

Active Gene ◽

U2 Snrnp ◽

Tight Linkage ◽

Polytene Nuclei

We describe the dynamic organization of pre-mRNA splicing factors in the intact polytene nuclei of the dipteran Chironomus tentans. The snRNPs and an SR non-snRNP splicing factor are present in excess, mainly distributed throughout the interchromatin. Approximately 10% of the U2 snRNP and an SR non-snRNP splicing factor are associated with the chromosomes, highly enriched in active gene loci where they are bound to RNA. We demonstrate that the splicing factors are specifically recruited to a defined gene upon induction of transcription during physiological conditions. Concomitantly, the splicing factors leave gene loci in which transcription is turned off. We also demonstrated that upon general transcription inhibition, the splicing factors redistribute from active gene loci to the interchromatin. Our findings demonstrate the dynamic intranuclear organization of splicing factors and a tight linkage between transcription and the intranuclear organization of the splicing machinery.

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Phenotyping sorghum [Sorghum bicolor (L.) Moench] for drought tolerance with special emphasis to root angle

African Journal of Agricultural Research ◽

10.5897/ajar2020.14801 ◽

2020 ◽

Vol 16 (8) ◽

pp. 1213-1222

Author(s):

Girma Firezer ◽

Mekbib Firew ◽

Tadesse Taye ◽

Menamo Temesgen ◽

Bantte Kassahun

Keyword(s):

Drought Tolerance ◽

Sorghum Bicolor ◽

Root Angle ◽

Sorghum Bicolor L

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Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: A possible regulation of splicing by a complex formation

International Journal of Cancer ◽

10.1002/ijc.1391 ◽

2001 ◽

Vol 93 (5) ◽

pp. 623-628 ◽

Cited By ~ 21

Author(s):

Kenji Harada ◽

Akira Yamada ◽

Damu Yang ◽

Kyogo Itoh ◽

Shigeki Shichijo

Keyword(s):

Complex Formation ◽

Mrna Splicing ◽

Tumor Rejection ◽

Splicing Factor ◽

Tumor Rejection Antigen

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The dynamics of a pre-mRNA splicing factor in living cells

Nature ◽

10.1038/387523a0 ◽

1997 ◽

Vol 387 (6632) ◽

pp. 523-527 ◽

Cited By ~ 387

Author(s):

Tom Misteli ◽

Javier F. Cáceres ◽

David L. Spector

Keyword(s):

Living Cells ◽

Mrna Splicing ◽

Splicing Factor

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In Silico Analysis of a Highly Mutated Gene in Cancer Provides Insight into Abnormal mRNA Splicing: Splicing Factor 3B Subunit 1K700E Mutant

Biomolecules ◽

10.3390/biom10050680 ◽

2020 ◽

Vol 10 (5) ◽

pp. 680 ◽

Cited By ~ 2

Author(s):

Asmaa Samy ◽

Baris Suzek ◽

Mehmet Ozdemir ◽

Ozge Sensoy

Keyword(s):

Rna Splicing ◽

In Silico Analysis ◽

Therapy Resistance ◽

Mrna Splicing ◽

Splicing Factor ◽

Cancer Types ◽

Dynamics Simulations ◽

Aberrant Rna ◽

The Impact ◽

Splicing Machinery

Cancer is the second leading cause of death worldwide. The etiology of the disease has remained elusive, but mutations causing aberrant RNA splicing have been considered one of the significant factors in various cancer types. The association of aberrant RNA splicing with drug/therapy resistance further increases the importance of these mutations. In this work, the impact of the splicing factor 3B subunit 1 (SF3B1) K700E mutation, a highly prevalent mutation in various cancer types, is investigated through molecular dynamics simulations. Based on our results, K700E mutation increases flexibility of the mutant SF3B1. Consequently, this mutation leads to i) disruption of interaction of pre-mRNA with SF3B1 and p14, thus preventing proper alignment of mRNA and causing usage of abnormal 3’ splice site, and ii) disruption of communication in critical regions participating in interactions with other proteins in pre-mRNA splicing machinery. We anticipate that this study enhances our understanding of the mechanism of functional abnormalities associated with splicing machinery, thereby, increasing possibility for designing effective therapies to combat cancer at an earlier stage.

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Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones

The Journal of Cell Biology ◽

10.1083/jcb.201701165 ◽

2017 ◽

Vol 216 (6) ◽

pp. 1579-1596 ◽

Cited By ~ 26

Author(s):

Anna Malinová ◽

Zuzana Cvačková ◽

Daniel Matějů ◽

Zuzana Hořejší ◽

Claire Abéza ◽

...

Keyword(s):

Quantitative Proteomics ◽

Mrna Splicing ◽

Splicing Factor ◽

Dependent Manner ◽

Proteomics Data ◽

Small Nuclear Ribonucleoprotein ◽

Crucial Component ◽

Potential Link ◽

Nuclear Ribonucleoprotein ◽

New Interactions

Splicing is catalyzed by the spliceosome, a complex of five major small nuclear ribonucleoprotein particles (snRNPs). The pre-mRNA splicing factor PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a central module of the spliceosome. Using quantitative proteomics, we identified assembly intermediates containing PRPF8, EFTUD2, and SNRNP200 in association with the HSP90/R2TP complex, its ZNHIT2 cofactor, and additional proteins. HSP90 and R2TP bind unassembled U5 proteins in the cytoplasm, stabilize them, and promote the formation of the U5 snRNP. We further found that PRPF8 mutants causing Retinitis pigmentosa assemble less efficiently with the U5 snRNP and bind more strongly to R2TP, with one mutant retained in the cytoplasm in an R2TP-dependent manner. We propose that the HSP90/R2TP chaperone system promotes the assembly of a key module of U5 snRNP while assuring the quality control of PRPF8. The proteomics data further reveal new interactions between R2TP and the tuberous sclerosis complex (TSC), pointing to a potential link between growth signals and the assembly of key cellular machines.

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