This Article
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 Sperling, R
Right arrow Articles by Kornberg, R D
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sperling, R
Right arrow Articles by Kornberg, R D

 Previous Article  |  Next Article 

Mol Cell Biol. 1985 March; 5(3): 569-575

Abundant nuclear ribonucleoprotein form of CAD RNA.

R Sperling, J Sperling, A D Levine, P Spann, G R Stark and R D Kornberg

ABSTRACT

Transcripts of the CAD gene in Syrian hamster cells are as abundant in the nucleus as in the cytoplasm. This was shown by in situ hybridization of whole cells and by solution and blot hybridization of subcellular fractions. Similar results were obtained both for wild-type cells and for a mutant containing amplified CAD genes in which the level of CAD RNA is 150-fold greater. CAD nuclear RNA is indistinguishable from mature mRNA by gel electrophoresis and blot hybridization. Discrete higher-molecular-weight precursors are undetectable, although the persistence of a short length of intervening sequence in the otherwise fully processed RNA is not excluded. CAD RNA is released from nuclei by sonication in physiological conditions in a ribonucleoprotein form that sediments as a broad peak at about 200S in a sucrose gradient. CAD sequences extracted from nuclei by treatment with EDTA and RNase are found in the 30S particles previously described.


Mol Cell Biol. 1985 March; 5(3): 569-575




This article has been cited by other articles:

  • Heinrich, B., Zhang, Z., Raitskin, O., Hiller, M., Benderska, N., Hartmann, A. M., Bracco, L., Elliott, D., Ben-Ari, S., Soreq, H., Sperling, J., Sperling, R., Stamm, S. (2009). Heterogeneous Nuclear Ribonucleoprotein G Regulates Splice Site Selection by Binding to CC(A/C)-rich Regions in Pre-mRNA. J. Biol. Chem. 284: 14303-14315 [Abstract] [Full Text]  
  • Chen, Y.-I G., Moore, R. E., Ge, H. Y., Young, M. K., Lee, T. D., Stevens, S. W. (2007). Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes expands the catalog of participating factors. Nucleic Acids Res 35: 3928-3944 [Abstract] [Full Text]  
  • Grunwald, D., Spottke, B., Buschmann, V., Kubitscheck, U. (2006). Intranuclear Binding Kinetics and Mobility of Single Native U1 snRNP Particles in Living Cells. Mol. Biol. Cell 17: 5017-5027 [Abstract] [Full Text]  
  • Iborra, F., Jackson, D., Cook, P. (1998). The path of transcripts from extra-nucleolar synthetic sites to nuclear pores: transcripts in transit are concentrated in discrete structures containing SR proteins. J. Cell Sci. 111: 2269-2282 [Abstract]  
  • Choi, Y., Grabowski, P., Sharp, P., Dreyfuss, G (1986). Heterogeneous nuclear ribonucleoproteins: role in RNA splicing. Science 231: 1534-1539 [Abstract]  
  • Raitskin, O., Cho, D.-S. C., Sperling, J., Nishikura, K., Sperling, R. (2001). RNA editing activity is associated with splicing factors in lnRNP particles: The nuclear pre-mRNA processing machinery. Proc. Natl. Acad. Sci. USA 98: 6571-6576 [Abstract] [Full Text]