Mol Cell Biol. 1989 September; 9(9): 3698-3709
PRP4 (RNA4) from Saccharomyces cerevisiae: its gene product is associated with the U4/U6 small nuclear ribonucleoprotein particle.
S P Bjørn,
A Soltyk,
J D Beggs and
J D Friesen
Hospital for Sick Children, Toronto, Ontario, Canada.
ABSTRACT
The PRP4 (RNA4) gene product is involved in nuclear mRNA processing in yeast cells; we have previously cloned the gene by complementation of a temperature-sensitive mutation. Sequence and transcript analyses of the cloned gene predicted the gene product to be a 52-kilodalton protein, which was confirmed with antibodies raised against the PRP4 gene product. These antibodies inhibited precursor mRNA splicing in vitro, demonstrating a direct role of PRP4 in splicing. Immunoprecipitations with the antibodies indicated that the PRP4 protein is associated with the U4/U6 small nuclear ribonucleoprotein particle.
Mol Cell Biol. 1989 September; 9(9): 3698-3709
This article has been cited by other articles:
-
Zhang, Z., Shen, X., Jones, B. H, Xu, B., Herr, J. C, Strauss, J. F III
(2008). Phosphorylation of Mouse Sperm Axoneme Central Apparatus Protein SPAG16L by a Testis-Specific Kinase, TSSK2. Biol. Reprod.
79: 75-83
[Abstract]
[Full Text]
-
Clark, T. A., Sugnet, C. W., Ares, M. Jr.
(2002). Genomewide Analysis of mRNA Processing in Yeast Using Splicing-Specific Microarrays. Science
296: 907-910
[Abstract]
[Full Text]
-
Lukowiak, A. A., Granneman, S., Mattox, S. A., Speckmann, W. A., Jones, K., Pluk, H., Venrooij, W. J. v., Terns, R. M., Terns, M. P.
(2000). Interaction of the U3-55k protein with U3 snoRNA is mediated by the Box B/C motif of U3 and the WD repeats of U3-55k. Nucleic Acids Res
28: 3462-3471
[Abstract]
[Full Text]
-
Achsel, T., Ahrens, K., Brahms, H., Teigelkamp, S., Lührmann, R.
(1998). The Human U5-220kD Protein (hPrp8) Forms a Stable RNA-Free Complex with Several U5-Specific Proteins, Including an RNA Unwindase, a Homologue of Ribosomal Elongation Factor EF-2, and a Novel WD-40 Protein. Mol. Cell. Biol.
18: 6756-6766
[Abstract]
[Full Text]
-
Chen, H.-R., Jan, S.-P., Tsao, T. Y., Sheu, Y.-J., Banroques, J., Cheng, S.-C.
(1998). Snt309p, a Component of the Prp19p-Associated Complex That Interacts with Prp19p and Associates with the Spliceosome Simultaneously with or Immediately after Dissociation of U4 in the Same Manner as Prp19p. Mol. Cell. Biol.
18: 2196-2204
[Abstract]
[Full Text]
-
Pluk, H., Soffner, J., Lührmann, R., Venrooij, W. J. v.
(1998). cDNA Cloning and Characterization of the Human U3 Small Nucleolar Ribonucleoprotein Complex-Associated 55-Kilodalton Protein. Mol. Cell. Biol.
18: 488-498
[Abstract]
[Full Text]
-
Horowitz, D S, Krainer, A R
(1997). A human protein required for the second step of pre-mRNA splicing is functionally related to a yeast splicing factor.. Genes Dev.
11: 139-151
[Abstract]
-
Fabrizio, P, Esser, S, Kastner, B, Luhrmann, R
(1994). Isolation of S. cerevisiae snRNPs: comparison of U1 and U4/U6.U5 to their human counterparts. Science
264: 261-265
[Abstract]
-
Ruby, S W, Chang, T H, Abelson, J
(1993). Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA.. Genes Dev.
7: 1909-1925
[Abstract]
-
Horowitz, D S, Abelson, J
(1993). Stages in the second reaction of pre-mRNA splicing: the final step is ATP independent.. Genes Dev.
7: 320-329
[Abstract]
-
Behrens, S E, Luhrmann, R
(1991). Immunoaffinity purification of a [U4/U6.U5] tri-snRNP from human cells.. Genes Dev.
5: 1439-1452
[Abstract]
-
Guthrie, C
(1991). Messenger RNA splicing in yeast: clues to why the spliceosome is a ribonucleoprotein. Science
253: 157-163
[Abstract]
-
Bordonne, R, Banroques, J, Abelson, J, Guthrie, C
(1990). Domains of yeast U4 spliceosomal RNA required for PRP4 protein binding, snRNP-snRNP interactions, and pre-mRNA splicing in vivo.. Genes Dev.
4: 1185-1196
[Abstract]
-
Fabrizio, P, McPheeters, D S, Abelson, J
(1989). In vitro assembly of yeast U6 snRNP: a functional assay.. Genes Dev.
3: 2137-2150
[Abstract]
Copyright © 1989 by the American Society for Microbiology. All rights reserved.