scholarly journals Identification and characterization of yUAP/Sub2p, a yeast homolog of the essential human pre-mRNA splicing factor hUAP56

2001 ◽  
Vol 15 (1) ◽  
pp. 30-35 ◽  
Author(s):  
M. Zhang
Keyword(s):  
Mrna Splicing ◽  
Splicing Factor ◽  
Yeast Homolog ◽  
Identification And Characterization

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 Myb-Related Fission Yeast cdc5p Is a Component of a 40S snRNP-Containing Complex and Is Essential for Pre-mRNA Splicing

1999 ◽  
Vol 19 (8) ◽  
pp. 5352-5362 ◽  
Author(s):  
W. Hayes McDonald ◽  
Ryoma Ohi ◽  
Natalia Smelkova ◽  
David Frendewey ◽  
Kathleen L. Gould
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Fission Yeast ◽  
Genetic Interaction ◽  
Cell Cycle Control ◽  
Mrna Splicing ◽  
Splicing Factor ◽  
Immunoaffinity Purification ◽  
Snrnp Protein

ABSTRACT Myb-related cdc5p is required for G2/M progression in the yeast Schizosaccharomyces pombe. We report here that all detectable cdc5p is stably associated with a multiprotein 40S complex. Immunoaffinity purification has allowed the identification of 10 cwf (complexed with cdc5p) proteins. Two (cwf6p and cwf10p) are members of the U5 snRNP; one (cwf9p) is a core snRNP protein. cwf8p is the apparent ortholog of the Saccharomyces cerevisiaesplicing factor Prp19p. cwf1 + is allelic to theprp5 + gene defined by the S. pombesplicing mutant, prp5-1, and there is a strong negative genetic interaction between cdc5-120 andprp5-1. Five cwfs have not been recognized previously as important for either pre-mRNA splicing or cell cycle control. Further characterization of cwf1p, cwf2p, cwf3p, and cwf4p demonstrates that they are encoded by essential genes, cosediment with cdc5p at 40S, and coimmunoprecipitate with cdc5p. We further show that cdc5p associates with the U2, U5, and U6 snRNAs and that cells lackingcdc5 + function are defective in pre-mRNA splicing. These data raise the possibility that the cdc5p complex is an intermediate in the assembly or disassembly of an active S. pombe spliceosome.

scholarly journals Characterization of U2AF6, a Splicing Factor Related to U2AF35

2002 ◽  
Vol 22 (1) ◽  
pp. 221-230 ◽  
Author(s):  
Jeremiah Shepard ◽  
Martin Reick ◽  
Sara Olson ◽  
Brenton R. Graveley
Keyword(s):  
Sequence Similarity ◽  
Sr Proteins ◽  
Mrna Splicing ◽  
Splicing Factor ◽  
Physical Interaction ◽  
U2 Auxiliary Factor ◽  
Auxiliary Factor ◽  
Strong Sequence Similarity ◽  
Splicing Enhancer

ABSTRACT The essential splicing factor U2AF (U2 auxiliary factor) is a heterodimer composed of 65-kDa (U2AF65) and 35-kDa (U2AF35) subunits. U2AF35 has multiple functions in pre-mRNA splicing. First, U2AF35 has been shown to function by directly interacting with the AG at the 3′ splice site. Second, U2AF35 is thought to play a role in the recruitment of U2AF65 by serine-arginine-rich (SR) proteins in enhancer-dependent splicing. It has been proposed that the physical interaction between the arginine-serine-rich (RS) domain of U2AF35 and SR proteins is important for this activity. However, other data suggest that this may not be the case. Here, we report the identification of a mammalian gene that encodes a 26-kDa protein bearing strong sequence similarity to U2AF35, designated U2AF26. The N-terminal 187 amino acids of U2AF35 and U2AF26 are nearly identical. However, the C-terminal domain of U2AF26 lacks many characteristics of the U2AF35 RS domain and, therefore, might be incapable of interacting with SR proteins. We show that U2AF26 can associate with U2AF65 and can functionally substitute for U2AF35 in both constitutive and enhancer-dependent splicing, demonstrating that the RS domain of the small U2AF subunit is not required for splicing enhancer function. Finally, we show that U2AF26 functions by enhancing the binding of U2AF65 to weak 3′ splice sites. These studies identify U2AF26 as a mammalian splicing factor and demonstrate that distinct U2AF complexes can participate in pre-mRNA splicing. Based on its sequence and functional similarity to U2AF35, U2AF26 may play a role in regulating alternative splicing.

scholarly journals 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.

Identification and Characterization of AberrantGAAPre-mRNA Splicing in Pompe Disease Using a Generic Approach

2014 ◽  
Vol 36 (1) ◽  
pp. 57-68 ◽  
Author(s):  
Atze J. Bergsma ◽  
Marian Kroos ◽  
Marianne Hoogeveen-Westerveld ◽  
Dicky Halley ◽  
Ans T. van der Ploeg ◽  
...  
Keyword(s):  
Pompe Disease ◽  
Mrna Splicing ◽  
Identification And Characterization

scholarly journals Identification and characterization of three members of the human SR family of pre-mRNA splicing factors.

1995 ◽  
Vol 14 (17) ◽  
pp. 4336-4349 ◽  
Author(s):  
G. R. Screaton ◽  
J. F. Cáceres ◽  
A. Mayeda ◽  
M. V. Bell ◽  
M. Plebanski ◽  
...  
Keyword(s):  
Mrna Splicing ◽  
Splicing Factors ◽  
Identification And Characterization

scholarly journals Identification and characterization of a yeast homolog of U1 snRNP-specific protein C

1997 ◽  
Vol 16 (13) ◽  
pp. 4082-4091 ◽  
Author(s):  
Jie Tang ◽  
Nadja Abovich ◽  
Margaret L. Fleming ◽  
Bertrand Séraphin ◽  
Michael Rosbash
Keyword(s):  
Protein C ◽  
Specific Protein ◽  
U1 Snrnp ◽  
Yeast Homolog ◽  
Identification And Characterization

scholarly journals The function of the NineTeen Complex (NTC) in regulating spliceosome conformations and fidelity during pre-mRNA splicing

2010 ◽  
Vol 38 (4) ◽  
pp. 1110-1115 ◽  
Author(s):  
Rebecca Hogg ◽  
Joanne C. McGrail ◽  
Raymond T. O'Keefe
Keyword(s):  
Recent Work ◽  
Present Article ◽  
Essential Role ◽  
Mrna Splicing ◽  
Associated Proteins ◽  
Intron Removal ◽  
Identification And Characterization ◽  
Small Nuclear Ribonucleoproteins ◽  
Essential Support

The NineTeen Complex (NTC) of proteins associates with the spliceosome during pre-mRNA splicing and is essential for both steps of intron removal. The NTC and other NTC-associated proteins are recruited to the spliceosome where they participate in regulating the formation and progression of essential spliceosome conformations required for the two steps of splicing. It is now clear that the NTC is an integral component of active spliceosomes from yeast to humans and provides essential support for the spliceosomal snRNPs (small nuclear ribonucleoproteins). In the present article, we discuss the identification and characterization of the yeast NTC and review recent work in yeast that supports the essential role for this complex in the regulation and fidelity of splicing.

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