Previous Article | Next Article 
Mol Cell Biol. 1993 October; 13(10): 6102-6113
PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae.
J T Anderson,
M R Paddy and
M S Swanson
Department of Immunology and Medical Microbiology, College of Medicine, University of Florida, Gainesville 32610-0266.
ABSTRACT
Proteins that directly associate with nuclear polyadenylated RNAs, or heterogeneous nuclear RNA-binding proteins (hnRNPs), and those that associate with cytoplasmic mRNAs, or mRNA-binding proteins (mRNPs), play important roles in regulating gene expression at the posttranscriptional level. Previous work with a variety of eukaryotic cells has demonstrated that hnRNPs are localized predominantly within the nucleus whereas mRNPs are cytoplasmic. While studying proteins associated with polyadenylated RNAs in Saccharomyces cerevisiae, we discovered an abundant polyuridylate-binding protein, PUB1, which appears to be both an hnRNP and an mRNP. PUB1 and PAB1, the polyadenylate tail-binding protein, are the two major proteins cross-linked by UV light to polyadenylated RNAs in vivo. The deduced primary structure of PUB1 indicates that it is a member of the ribonucleoprotein consensus sequence family of RNA-binding proteins and is structurally related to the human hnRNP M proteins. Even though the PUB1 protein is a major cellular polyadenylated RNA-binding protein, it is nonessential for cell growth. Indirect cellular immunofluorescence combined with digital image processing allowed a detailed comparison of the intracellular distributions of PUB1 and PAB1. While PAB1 is predominantly, and relatively uniformly, distributed within the cytoplasm, PUB1 is localized in a nonuniform pattern throughout both the nucleus and the cytoplasm. The cytoplasmic distribution of PUB1 is considerably more discontinuous than that of PAB1. Furthermore, sucrose gradient sedimentation analysis demonstrates that PAB1 cofractionates with polyribosomes whereas PUB1 does not. These results suggest that PUB1 is both an hnRNP and an mRNP and that it may be stably bound to a translationally inactive subpopulation of mRNAs within the cytoplasm.
Mol Cell Biol. 1993 October; 13(10): 6102-6113
This article has been cited by other articles:
-
Apponi, L. H., Kelly, S. M., Harreman, M. T., Lehner, A. N., Corbett, A. H., Valentini, S. R.
(2007). An Interaction between Two RNA Binding Proteins, Nab2 and Pub1, Links mRNA Processing/Export and mRNA Stability. Mol. Cell. Biol.
27: 6569-6579
[Abstract]
[Full Text]
-
Dong, J., Lai, R., Jennings, J. L., Link, A. J., Hinnebusch, A. G.
(2005). The Novel ATP-Binding Cassette Protein ARB1 Is a Shuttling Factor That Stimulates 40S and 60S Ribosome Biogenesis. Mol. Cell. Biol.
25: 9859-9873
[Abstract]
[Full Text]
-
OZANICK, S., KRECIC, A., ANDERSLAND, J., ANDERSON, J. T.
(2005). The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans. RNA
11: 1281-1290
[Abstract]
[Full Text]
-
Duttagupta, R., Tian, B., Wilusz, C. J., Khounh, D. T., Soteropoulos, P., Ouyang, M., Dougherty, J. P., Peltz, S. W.
(2005). Global Analysis of Pub1p Targets Reveals a Coordinate Control of Gene Expression through Modulation of Binding and Stability. Mol. Cell. Biol.
25: 5499-5513
[Abstract]
[Full Text]
-
BRUNE, C., MUNCHEL, S. E., FISCHER, N., PODTELEJNIKOV, A. V., WEIS, K.
(2005). Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export. RNA
11: 517-531
[Abstract]
[Full Text]
-
Trautwein, M., Dengjel, J., Schirle, M., Spang, A.
(2004). Arf1p Provides an Unexpected Link between COPI Vesicles and mRNA in Saccharomyces cerevisiae. Mol. Biol. Cell
15: 5021-5037
[Abstract]
[Full Text]
-
Dong, J., Lai, R., Nielsen, K., Fekete, C. A., Qiu, H., Hinnebusch, A. G.
(2004). The Essential ATP-binding Cassette Protein RLI1 Functions in Translation by Promoting Preinitiation Complex Assembly. J. Biol. Chem.
279: 42157-42168
[Abstract]
[Full Text]
-
Lang, B. D., Li, A.-m., Black-Brewster, H. D., Fridovich-Keil, J. L.
(2001). The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast. Nucleic Acids Res
29: 2567-2574
[Abstract]
[Full Text]
-
Lang, B. D., Fridovich-Keil, J. L.
(2000). Scp160p, a multiple KH-domain protein, is a component of mRNP complexes in yeast. Nucleic Acids Res
28: 1576-1584
[Abstract]
[Full Text]
-
Gallouzi, I.-E., Brennan, C. M., Stenberg, M. G., Swanson, M. S., Eversole, A., Maizels, N., Steitz, J. A.
(2000). HuR binding to cytoplasmic mRNA is perturbed by heat shock. Proc. Natl. Acad. Sci. USA
97: 3073-3078
[Abstract]
[Full Text]
-
Bates, E. J., Knuepfer, E., Smith, D. F.
(2000). Poly(A)-binding protein I of Leishmania: functional analysis and localisation in trypanosomatid parasites. Nucleic Acids Res
28: 1211-1220
[Abstract]
[Full Text]
-
Tirupati, H. K., Shaw, L. C., Lewin, A. S.
(1999). An RNA Binding Motif in the Cbp2 Protein Required for Protein-stimulated RNA Catalysis. J. Biol. Chem.
274: 30393-30401
[Abstract]
[Full Text]
-
Anderson, J., Phan, L., Cuesta, R., Carlson, B. A., Pak, M., Asano, K., Björk, G. R., Tamame, M., Hinnebusch, A. G.
(1998). The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev.
12: 3650-3662
[Abstract]
[Full Text]
-
Brown, C. E., Sachs, A. B.
(1998). Poly(A) Tail Length Control in Saccharomyces cerevisiae Occurs by Message-Specific Deadenylation. Mol. Cell. Biol.
18: 6548-6559
[Abstract]
[Full Text]
-
Drysdale, C. M., Jackson, B. M., McVeigh, R., Klebanow, E. R., Bai, Y., Kokubo, T., Swanson, M., Nakatani, Y., Weil, P. A., Hinnebusch, A. G.
(1998). The Gcn4p Activation Domain Interacts Specifically In Vitro with RNA Polymerase II Holoenzyme, TFIID, and the Adap-Gcn5p Coactivator Complex. Mol. Cell. Biol.
18: 1711-1724
[Abstract]
[Full Text]
-
Minvielle-Sebastia, L., Preker, P. J., Wiederkehr, T., Strahm, Y., Keller, W.
(1997). The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation. Proc. Natl. Acad. Sci. USA
94: 7897-7902
[Abstract]
[Full Text]
-
Uesono, Y., Toh-e, A., Kikuchi, Y.
(1997). Ssd1p of Saccharomyces cerevisiae Associates with RNA. J. Biol. Chem.
272: 16103-16109
[Abstract]
[Full Text]
-
Yurkova, M. S., Murray, M. T.
(1997). A Translation Regulatory Particle Containing the Xenopus Oocyte Y Box Protein mRNP3+4. J. Biol. Chem.
272: 10870-10876
[Abstract]
[Full Text]
-
Caponigro, G, Parker, R
(1995). Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast.. Genes Dev.
9: 2421-2432
[Abstract]
Copyright © 1993 by the American Society for Microbiology. All rights reserved.