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

2001 ◽  
Vol 93 (5) ◽  
pp. 623-628 ◽  
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

Detection and characterization of a factor which rescues spliceosome assembly from a heat-inactivated HeLa cell nuclear extract

1991 ◽  
Vol 11 (7) ◽  
pp. 3425-3431
Author(s):  
P Delannoy ◽  
M H Caruthers
Keyword(s):  
Heat Treatment ◽  
Hela Cell ◽  
Nuclear Extract ◽  
Mrna Splicing ◽  
Splicing Factor ◽  
Nuclear Extracts ◽  
Small Nuclear Rnas ◽  
A Minor ◽  
Cell Nuclear Extract

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.

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

1996 ◽  
Vol 133 (5) ◽  
pp. 929-941 ◽  
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.

scholarly journals Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa

2010 ◽  
Vol 12 (3) ◽  
pp. 344-355 ◽  
Author(s):  
Duvvuri Butchi Kameshwari ◽  
Satish Bhande ◽  
Curam Sreenivasacharlu Sundaram ◽  
Venkatesh Kota ◽  
Archana B. Siva ◽  
...  
Keyword(s):  
Tumor Rejection ◽  
Protein Precursor ◽  
Tumor Rejection Antigen ◽  
Epididymal Spermatozoa ◽  
Glucose Regulated Protein

scholarly journals The gene coding for a major tumor rejection antigen of tumor P815 is identical to the normal gene of syngeneic DBA/2 mice.

1991 ◽  
Vol 173 (6) ◽  
pp. 1373-1384 ◽  
Author(s):  
B Van den Eynde ◽  
B Lethé ◽  
A Van Pel ◽  
E De Plaen ◽  
T Boon
Keyword(s):  
Mast Cell ◽  
Tumor Rejection ◽  
Cosmid Library ◽  
Adult Mice ◽  
Gene Coding ◽  
Tumor Rejection Antigen ◽  
Normal Gene ◽  
Mast Cell Line ◽  
High Level

We showed previously that mouse mastocytoma P815 expresses several distinct antigens that are recognized by cytolytic T lymphocytes (CTL) of syngeneic DBA/2 mice. Antigens P815A and P815B are usually lost jointly and are targets for immune rejection responses in vivo. We used a cosmid library and a CTL stimulation assay to obtain transfectants expressing tumor rejection antigen P815A. From these transfectants we retrieved gene P1A which transferred the expression of both P815A and B. This gene is unrelated to three previously isolated genes coding for tum-antigens. It encodes a putative protein of 224 amino acids which contains two highly acidic domains showing homology with similar regions of nuclear proteins. The P1A gene expressed by tumor P815 is completely identical to the gene present in normal DBA/2 cells. Expression of the gene was tested by Northern blots. Cells from liver, spleen, and a number of mast cell lines were negative, but mast cell line L138.8A produced a high level of P1A message and was lysed by CTL directed against antigens P815A and B. We conclude that major tumor rejection antigens of P815 are encoded by a gene showing little or no expression in most normal cells of adult mice.

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

Nature ◽  
1997 ◽  
Vol 387 (6632) ◽  
pp. 523-527 ◽  
Author(s):  
Tom Misteli ◽  
Javier F. Cáceres ◽  
David L. Spector
Keyword(s):  
Living Cells ◽  
Mrna Splicing ◽  
Splicing Factor

Expression of the SART1 tumor-rejection antigen in hepatocellular carcinomas

2001 ◽  
Author(s):  
S. Yutani ◽  
S. Shichijo ◽  
Y. Inoue ◽  
N. Kawagoe ◽  
K. Okuda ◽  
...  
Keyword(s):  
Tumor Rejection ◽  
Hepatocellular Carcinomas ◽  
Tumor Rejection Antigen

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

Biomolecules ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 680 ◽  
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.

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

2017 ◽  
Vol 216 (6) ◽  
pp. 1579-1596 ◽  
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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