Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 22 October 1993:
Vol. 262. no. 5133, pp. 573 - 575
DOI: 10.1126/science.8211184

Articles

Science, Vol 262, Issue 5133, 573-575
Copyright © 1993 by American Association for the Advancement of Science


articles

U2AF homolog required for splicing in vivo

J Potashkin, K Naik, and K Wentz-Hunter

Department of Pharmacology and Molecular Biology, University of Health Sciences, Chicago Medical School, IL 60064.

Several fission yeast temperature-sensitive mutants defective in pre-mRNA processing (prp- mutants) at the nonpermissive temperature have been identified. Here, the prp2+ gene has been cloned by its ability to complement the temperature-sensitive growth defect of a prp2- mutant. The gene also corrects the pre-mRNA splicing defect of prp2- mutants and encodes a 59-kilodalton polypeptide (PRP2). A molecular characterization indicates that PRP2 is a previously uncharacterized yeast splicing factor with extensive similarity to the mammalian splicing factor U2AF65. Thus, this study provides evidence that a U2AF homolog participates in RNA processing in vivo.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A Conditional Role of U2AF in Splicing of Introns with Unconventional Polypyrimidine Tracts.
V. Sridharan and R. Singh (2007)
Mol. Cell. Biol. 27, 7334-7344
   Abstract »    Full Text »    PDF »
The impact of alternative splicing in vivo: Mouse models show the way.
T. Moroy and F. Heyd (2007)
RNA 13, 1155-1171
   Abstract »    Full Text »    PDF »
Structural characterization of the fission yeast U5.U2/U6 spliceosome complex.
M. D. Ohi, L. Ren, J. S. Wall, K. L. Gould, and T. Walz (2007)
PNAS 104, 3195-3200
   Abstract »    Full Text »    PDF »
Analysis of Mutant Phenotypes and Splicing Defects Demonstrates Functional Collaboration between the Large and Small Subunits of the Essential Splicing Factor U2AF In Vivo.
C. J. Webb, S. Lakhe-Reddy, C. M. Romfo, and J. A. Wise (2005)
Mol. Biol. Cell 16, 584-596
   Abstract »    Full Text »    PDF »
Exonic splicing enhancers in fission yeast: functional conservation demonstrates an early evolutionary origin.
C. J. Webb, C. M. Romfo, W. J. van Heeckeren, and J. A. Wise (2005)
Genes & Dev. 19, 242-254
   Abstract »    Full Text »    PDF »
U2AF homology motifs: protein recognition in the RRM world.
C. L. Kielkopf, S. Lucke, and M. R. Green (2004)
Genes & Dev. 18, 1513-1526
   Abstract »    Full Text »    PDF »
The Splicing Factor U2AF Small Subunit Is Functionally Conserved between Fission Yeast and Humans.
C. J. Webb and J. A. Wise (2004)
Mol. Cell. Biol. 24, 4229-4240
   Abstract »    Full Text »    PDF »
The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF65) is essential in vivo but dispensable for activity in vitro.
H. BANERJEE, A. RAHN, B. GAWANDE, S. GUTH, J. VALCARCEL, and R. SINGH (2004)
RNA 10, 240-253
   Abstract »    Full Text »    PDF »
Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding.
H. BANERJEE, A. RAHN, W. DAVIS, and R. SINGH (2003)
RNA 9, 88-99
   Abstract »    Full Text »    PDF »
Conserved Wat1/Pop3 WD-repeat protein of fission yeast secures genome stability through microtubule integrity and may be involved in mRNA maturation.
I. L. Ochotorena, D. Hirata, K.-i. Kominami, J. Potashkin, F. Sahin, K. Wentz-Hunter, K. L. Gould, K. Sato, Y. Yoshida, L. Vardy, et al. (2002)
J. Cell Sci. 114, 2911-2920
   Abstract »    Full Text »    PDF »
Characterization of U2AF6, a Splicing Factor Related to U2AF35.
J. Shepard, M. Reick, S. Olson, and B. R. Graveley (2002)
Mol. Cell. Biol. 22, 221-230
   Abstract »    Full Text »    PDF »
Utilization of the Bovine Papillomavirus Type 1 Late-Stage-Specific Nucleotide 3605 3' Splice Site Is Modulated by a Novel Exonic Bipartite Regulator but Not by an Intronic Purine-Rich Element.
Z.-M. Zheng, E. S. Reid, and C. C. Baker (2000)
J. Virol. 74, 10612-10622
   Abstract »    Full Text »
Evidence for Splice Site Pairing via Intron Definition in Schizosaccharomyces pombe.
C. M. Romfo, C. J. Alvarez, W. J. van Heeckeren, C. J. Webb, and J. A. Wise (2000)
Mol. Cell. Biol. 20, 7955-7970
   Abstract »    Full Text »
SURVEY AND SUMMARY: Analysis of the splicing machinery in fission yeast: a comparison with budding yeast and mammals.
N. F. Kaufer and J. Potashkin (2000)
Nucleic Acids Res. 28, 3003-3010
   Abstract »    Full Text »    PDF »
Optimization of a Weak 3' Splice Site Counteracts the Function of a Bovine Papillomavirus Type 1 Exonic Splicing Suppressor In Vitro and In Vivo.
Z.-M. Zheng, J. Quintero, E. S. Reid, C. Gocke, and C. C. Baker (2000)
J. Virol. 74, 5902-5910
   Abstract »    Full Text »
Biochemical and Genetic Conservation of Fission Yeast Dsk1 and Human SR Protein-Specific Kinase 1.
Z. Tang, T. Kuo, J. Shen, and R.-J. Lin (2000)
Mol. Cell. Biol. 20, 816-824
   Abstract »    Full Text »
spp42, Identified as a Classical Suppressor of prp4-73, Which Encodes a Kinase Involved in Pre-mRNA Splicing in Fission Yeast, Is a Homologue of the Splicing Factor Prp8p.
H. Schmidt, K. Richert, R. A. Drakas, and N. F. Käufer (1999)
Genetics 153, 1183-1191
   Abstract »    Full Text »
Characterization of the ptr6+ Gene in Fission Yeast: A Possible Involvement of a Transcriptional Coactivator TAF in Nucleocytoplasmic Transport of mRNA.
T. Shibuya, S. Tsuneyoshi, A. K. Azad, S. Urushiyama, Y. Ohshima, and T. Tani (1999)
Genetics 152, 869-880
   Abstract »    Full Text »
CUS2, a Yeast Homolog of Human Tat-SF1, Rescues Function of Misfolded U2 through an Unusual RNA Recognition Motif.
D. Yan, R. Perriman, H. Igel, K. J. Howe, M. Neville, and M. Ares Jr. (1998)
Mol. Cell. Biol. 18, 5000-5009
   Abstract »    Full Text »
A Potential Role for U2AF-SAP 155 Interactions in Recruiting U2 snRNP to the Branch Site.
O. Gozani, J. Potashkin, and R. Reed (1998)
Mol. Cell. Biol. 18, 4752-4760
   Abstract »    Full Text »
Genetic analysis of the SR protein ASF/SF2: interchangeability of RS domains and negative control of splicing.
J. Wang, S.-H. Xiao, and J. L. Manley (1998)
Genes & Dev. 12, 2222-2233
   Abstract »    Full Text »
RNA Binding Activity of Heterodimeric Splicing Factor U2AF: at Least One RS Domain Is Required for High-Affinity Binding.
D. Z. Rudner, K. S. Breger, R. Kanaar, M. D. Adams, and D. C. Rio (1998)
Mol. Cell. Biol. 18, 4004-4011
   Abstract »    Full Text »
Interaction between Subunits of Heterodimeric Splicing Factor U2AF Is Essential In Vivo.
D. Z. Rudner, R. Kanaar, K. S. Breger, and D. C. Rio (1998)
Mol. Cell. Biol. 18, 1765-1773
   Abstract »    Full Text »
Molecular genetic analysis of the heterodimeric splicing factor U2AF: the RS domain on either the large or small Drosophila subunit is dispensable in vivo.
D. Z. Rudner, K. S. Breger, and D. C. Rio (1998)
Genes & Dev. 12, 1010-1021
   Abstract »    Full Text »
Fission Yeast Mitotic Regulator Dsk1 Is an SR Protein-specific Kinase.
Z. Tang, M. Yanagida, and R.-J. Lin (1998)
J. Biol. Chem. 273, 5963-5969
   Abstract »    Full Text »    PDF »
SRPK2: A Differentially Expressed SR Protein-specific Kinase Involved in Mediating the Interaction and Localization of Pre-mRNA Splicing Factors in Mammalian Cells.
H.-Y. Wang, W. Lin, J. A. Dyck, J. M. Yeakley, Z. Songyang, L. C. Cantley, and X.-D. Fu (1998)
J. Cell Biol. 140, 737-750
   Abstract »    Full Text »    PDF »
KIS Is a Protein Kinase with an RNA Recognition Motif.
A. Maucuer, S. Ozon, V. Manceau, O. Gavet, S. Lawler, P. Curmi, and A. Sobel (1997)
J. Biol. Chem. 272, 23151-23156
   Abstract »    Full Text »    PDF »
U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction..
J Fleckner, M Zhang, J Valcarcel, and M R Green (1997)
Genes & Dev. 11, 1864-1872
   Abstract »    PDF »
Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins.
R Singh, J Valcarcel, and M. Green (1995)
Science 268, 1173-1176
   Abstract »    PDF »
The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition..
N Abovich, X C Liao, and M Rosbash (1994)
Genes & Dev. 8, 843-854
   Abstract »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)