This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Windgassen, M.
Right arrow Articles by Krebber, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Windgassen, M.
Right arrow Articles by Krebber, H.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, December 2004, p. 10479-10491, Vol. 24, No. 23
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.23.10479-10491.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Yeast Shuttling SR Proteins Npl3p, Gbp2p, and Hrb1p Are Part of the Translating mRNPs, and Npl3p Can Function as a Translational Repressor

Merle Windgassen,1,{dagger} Dorothée Sturm,1,{dagger} Iván J. Cajigas,2 Carlos I. González,2 Matthias Seedorf,3 Holger Bastians,1 and Heike Krebber1*

Institut für Molekularbiologie und Tumorforschung der Philipps-Universität Marburg, Marburg,1 Zentrum für Molekulare Biologie der Universität in Heidelberg, Heidelberg, Germany,3 Department of Biology, University of Puerto Rico—Río Piedras, San Juan, Puerto Rico2

Received 3 June 2004/ Returned for modification 8 July 2004/ Accepted 7 September 2004

A major challenge in current molecular biology is to understand how sequential steps in gene expression are coupled. Recently, much attention has been focused on the linkage of transcription, processing, and mRNA export. Here we describe the cytoplasmic rearrangement for shuttling mRNA binding proteins in Saccharomyces cerevisiae during translation. While the bulk of Hrp1p, Nab2p, or Mex67p is not associated with polysome containing mRNAs, significant amounts of the serine/arginine (SR)-type shuttling mRNA binding proteins Npl3p, Gbp2p, and Hrb1p remain associated with the mRNA-protein complex during translation. Interestingly, a prolonged association of Npl3p with polysome containing mRNAs results in translational defects, indicating that Npl3p can function as a negative translational regulator. Consistent with this idea, a mutation in NPL3 that slows down translation suppresses growth defects caused by the presence of translation inhibitors or a mutation in eIF5A. Moreover, using sucrose density gradient analysis, we provide evidence that the import receptor Mtr10p, but not the SR protein kinase Sky1p, is involved in the timely regulated release of Npl3p from polysome-associated mRNAs. Together, these data shed light onto the transformation of an exporting to a translating mRNP.

* Corresponding author. Mailing address: Institut für Molekularbiologie und Tumorforschung (IMT) der Philipps-Universität Marburg, Emil-Mannkopff-Str. 2, 35037 Marburg, Germany. Phone: 49 6421 286 6773. Fax: 49 6421 286 5932. E-mail: krebber{at}imt.uni-marburg.de.

{dagger} M.W. and D.S. contributed equally to this work.

Molecular and Cellular Biology, December 2004, p. 10479-10491, Vol. 24, No. 23
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.23.10479-10491.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Dossani, Z. Y., Weirich, C. S., Erzberger, J. P., Berger, J. M., Weis, K. (2009). Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1. Proc. Natl. Acad. Sci. USA 106: 16251-16256 [Abstract] [Full Text]  
  • McBride, A. E., Conboy, A. K., Brown, S. P., Ariyachet, C., Rutledge, K. L. (2009). Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function. Nucleic Acids Res 37: 4322-4330 [Abstract] [Full Text]  
  • Zhang, X.-N., Mount, S. M. (2009). Two Alternatively Spliced Isoforms of the Arabidopsis SR45 Protein Have Distinct Roles during Normal Plant Development. Plant Physiol. 150: 1450-1458 [Abstract] [Full Text]  
  • Lemieux, C., Bachand, F. (2009). Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs. Nucleic Acids Res 37: 3418-3430 [Abstract] [Full Text]  
  • Bjork, P., Jin, S., Zhao, J., Singh, O. P., Persson, J.-O., Hellman, U., Wieslander, L. (2009). Specific combinations of SR proteins associate with single pre-messenger RNAs in vivo and contribute different functions. JCB 184: 555-568 [Abstract] [Full Text]  
  • Lund, M. K., Kress, T. L., Guthrie, C. (2008). Autoregulation of Npl3, a Yeast SR Protein, Requires a Novel Downstream Region and Serine Phosphorylation. Mol. Cell. Biol. 28: 3873-3881 [Abstract] [Full Text]  
  • Farny, N. G., Hurt, J. A., Silver, P. A. (2008). Definition of global and transcript-specific mRNA export pathways in metazoans. Genes Dev. 22: 66-78 [Abstract] [Full Text]  
  • 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]  
  • Swartz, J. E., Bor, Y.-C., Misawa, Y., Rekosh, D., Hammarskjold, M.-L. (2007). The Shuttling SR Protein 9G8 Plays a Role in Translation of Unspliced mRNA Containing a Constitutive Transport Element. J. Biol. Chem. 282: 19844-19853 [Abstract] [Full Text]  
  • Rother, S., Strasser, K. (2007). The RNA polymerase II CTD kinase Ctk1 functions in translation elongation. Genes Dev. 21: 1409-1421 [Abstract] [Full Text]  
  • Guil, S., Long, J. C., Caceres, J. F. (2006). hnRNP A1 Relocalization to the Stress Granules Reflects a Role in the Stress Response. Mol. Cell. Biol. 26: 5744-5758 [Abstract] [Full Text]  
  • Izquierdo, J.-M., Valcarcel, J. (2006). A simple principle to explain the evolution of pre-mRNA splicing.. Genes Dev. 20: 1679-1684 [Full Text]  
  • Butterfield-Gerson, K. L., Scheifele, L. Z., Ryan, E. P., Hopper, A. K., Parent, L. J. (2006). Importin-{beta} Family Members Mediate Alpharetrovirus Gag Nuclear Entry via Interactions with Matrix and Nucleocapsid. J. Virol. 80: 1798-1806 [Abstract] [Full Text]  
  • McBride, A. E., Cook, J. T., Stemmler, E. A., Rutledge, K. L., McGrath, K. A., Rubens, J. A. (2005). Arginine Methylation of Yeast mRNA-binding Protein Npl3 Directly Affects Its Function, Nuclear Export, and Intranuclear Protein Interactions. J. Biol. Chem. 280: 30888-30898 [Abstract] [Full Text]  
  • KIM GUISBERT, K., DUNCAN, K., LI, H., GUTHRIE, C. (2005). Functional specificity of shuttling hnRNPs revealed by genome-wide analysis of their RNA binding profiles. RNA 11: 383-393 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»