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 Tang, H.
Right arrow Articles by Wong-Staal, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tang, H.
Right arrow Articles by Wong-Staal, F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, May 1999, p. 3540-3550, Vol. 19, No. 5
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Carboxyl Terminus of RNA Helicase A Contains a Bidirectional Nuclear Transport Domain

Hengli Tang,1 David McDonald, Tamara Middlesworth,1 Thomas J. Hope, and Flossie Wong-Staal1,*

Department of Biology1 and Department of Medicine,3 University of California, San Diego, and Infectious Disease Laboratory, The Salk Institute for Biological Sciences,2 La Jolla, California

Received 31 August 1998/Returned for modification 5 October 1998/Accepted 29 January 1999

Human RNA helicase A was recently identified to be a shuttle protein which interacts with the constitutive transport element (CTE) of type D retroviruses. Here we show that a domain of 110 amino acids at the carboxyl terminus of helicase A is both necessary and sufficient for nuclear localization as well as rapid nuclear export of glutathione S-transferase fusion proteins. The import and export activities of this domain overlap but are separable by point mutations. This bidirectional nuclear transport domain (NTD) has no obvious sequence homology to previously identified nuclear import or export signals. However, the Ran-dependent nuclear import of NTD was efficiently competed by excess amounts of the nuclear localization signal (NLS) peptide from simian virus 40 large T antigen, suggesting that import is mediated by the classical NLS pathway. The nuclear export pathway accessed by NTD is insensitive to leptomycin B and thus is distinct from the leucine-rich nuclear export signal pathway mediated by CRM1.

* Corresponding author. Mailing address: Stein Clinical Research Building, University of California, San Diego, La Jolla, CA 92093-0665. Phone: (619) 534-7957. Fax: (619) 534-7743. E-mail: fwongstaal{at}ucsd.edu.

Molecular and Cellular Biology, May 1999, p. 3540-3550, Vol. 19, No. 5
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Lawrence, P., Rieder, E. (2009). Identification of RNA Helicase A as a New Host Factor in the Replication Cycle of Foot-and-Mouth Disease Virus. J. Virol. 83: 11356-11366 [Abstract] [Full Text]  
  • Groom, H. C. T., Anderson, E. C., Lever, A. M. L. (2009). Rev: beyond nuclear export. J. Gen. Virol. 90: 1303-1318 [Abstract] [Full Text]  
  • Izzo, A., Regnard, C., Morales, V., Kremmer, E., Becker, P. B. (2008). Structure-function analysis of the RNA helicase maleless. Nucleic Acids Res 36: 950-962 [Abstract] [Full Text]  
  • Fuller-Pace, F. V. (2006). DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res 34: 4206-4215 [Abstract] [Full Text]  
  • Roy, B. B., Hu, J., Guo, X., Russell, R. S., Guo, F., Kleiman, L., Liang, C. (2006). Association of RNA Helicase A with Human Immunodeficiency Virus Type 1 Particles. J. Biol. Chem. 281: 12625-12635 [Abstract] [Full Text]  
  • Smith, W. A., Schurter, B. T., Wong-Staal, F., David, M. (2004). Arginine Methylation of RNA Helicase A Determines Its Subcellular Localization. J. Biol. Chem. 279: 22795-22798 [Abstract] [Full Text]  
  • Gill, S. K., Bhattacharya, M., Ferguson, S. S. G., Rylett, R. J. (2003). Identification of a Novel Nuclear Localization Signal Common to 69- and 82-kDa Human Choline Acetyltransferase. J. Biol. Chem. 278: 20217-20224 [Abstract] [Full Text]  
  • Jackman, M., Kubota, Y., den Elzen, N., Hagting, A., Pines, J. (2002). Cyclin A- and Cyclin E-Cdk Complexes Shuttle between the Nucleus and the Cytoplasm. Mol. Biol. Cell 13: 1030-1045 [Abstract] [Full Text]  
  • Zhang, S., Buder, K., Burkhardt, C., Schlott, B., Gorlach, M., Grosse, F. (2002). Nuclear DNA Helicase II/RNA Helicase A Binds to Filamentous Actin. J. Biol. Chem. 277: 843-853 [Abstract] [Full Text]  
  • Sanjuán, R., Marín, I. (2001). Tracing the Origin of the Compensasome: Evolutionary History of DEAH Helicase and MYST Acetyltransferase Gene Families. Mol Biol Evol 18: 330-343 [Abstract] [Full Text]  
  • Mendell, J. T., Medghalchi, S. M., Lake, R. G., Noensie, E. N., Dietz, H. C. (2000). Novel Upf2p Orthologues Suggest a Functional Link between Translation Initiation and Nonsense Surveillance Complexes. Mol. Cell. Biol. 20: 8944-8957 [Abstract] [Full Text]  
  • Askjaer, P., Rosendahl, R., Kjems, J. (2000). Nuclear Export of the DEAD Box An3 Protein by CRM1 Is Coupled to An3 Helicase Activity. J. Biol. Chem. 275: 11561-11568 [Abstract] [Full Text]  
  • Liu, J., DeFranco, D. B. (2000). Protracted Nuclear Export of Glucocorticoid Receptor Limits Its Turnover and Does Not Require the Exportin 1/CRM1-Directed Nuclear Export Pathway. Mol. Endocrinol. 14: 40-51 [Abstract] [Full Text]  
  • Tang, H., Wong-Staal, F. (2000). Specific Interaction between RNA Helicase A and Tap, Two Cellular Proteins That Bind to the Constitutive Transport Element of Type D Retrovirus. J. Biol. Chem. 275: 32694-32700 [Abstract] [Full Text]  
  • Myohanen, S., Baylin, S. B. (2001). Sequence-specific DNA Binding Activity of RNA Helicase A to the p16INK4a Promoter. J. Biol. Chem. 276: 1634-1642 [Abstract] [Full Text]  
  • Yang, J.-P., Tang, H., Reddy, T. R., Wong-Staal, F. (2001). Mapping the Functional Domains of HAP95, a Protein That Binds RNA Helicase A and Activates the Constitutive Transport Element of Type D Retroviruses. J. Biol. Chem. 276: 30694-30700 [Abstract] [Full Text]  
  • Westberg, C., Yang, J.-P., Tang, H., Reddy, T. R., Wong-Staal, F. (2000). A Novel Shuttle Protein Binds to RNA Helicase A and Activates the Retroviral Constitutive Transport Element. J. Biol. Chem. 275: 21396-21401 [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»