This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Maraia, R Articles by Adeniyi-Jones, S Search for Related Content PubMed PubMed Citation Articles by Maraia, R Articles by Adeniyi-Jones, S

 Previous Article  |  Next Article 

Mol Cell Biol. 1988 October; 8(10): 4433-4440

Pathway of B1-Alu expression in microinjected oocytes: Xenopus laevis proteins associated with nuclear precursor and processed cytoplasmic RNAs.

Human Genetics Branch, National Institute of Child Health and Human Development, Bethesda, Maryland 20892.

ABSTRACT

We have previously characterized B1-Alu gene expression by microinjected Xenopus laevis oocytes. The transcription, endonucleolytic processing and its kinetics, nuclear transport kinetics, and subsequent cellular compartmentalization have been described previously (Adeniyi-Jones and Zasloff, Nature 317:81-84, 1985). Briefly, a B1-Alu gene is transcribed by RNA polymerase III to a 210-nucleotide (210nt) primary transcript which is processed to yield 135nt and 75nt RNAs. After processing, the 135nt RNA enters the cytoplasmic compartment, where it remains stable, while the 75nt RNA is degraded. In this report we characterize this pathway further and show that the RNAs involved are complexed with specific X. laevis proteins. The primary transcript was associated with an X. laevis protein of 63 kilodaltons (p63) as well as La, a protein known to be associated with RNA polymerase III transcripts. After processing, the cytoplasmic 135nt RNA remained associated only with the X. laevis p63 in the form of a small ribonucleoprotein. Human autoimmune antibodies were purified by affinity chromatography to X. laevis p63 and used to immunoprecipitate human ribonucleoprotein containing a 63-kilodalton polypeptide and small RNAs. These data suggest that Alu-analogous ribonucleoproteins and their metabolic pathways are conserved across species and provide insight as to their possible functions.

This article has been cited by other articles:

• Krueger, B. J., Jeronimo, C., Roy, B. B., Bouchard, A., Barrandon, C., Byers, S. A., Searcey, C. E., Cooper, J. J., Bensaude, O., Cohen, E. A., Coulombe, B., Price, D. H. (2008). LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated. Nucleic Acids Res 36: 2219-2229 [Abstract] [Full Text]  
• Intine, R. V., Dundr, M., Vassilev, A., Schwartz, E., Zhao, Y., Zhao, Y., DePamphilis, M. L., Maraia, R. J. (2004). Nonphosphorylated Human La Antigen Interacts with Nucleolin at Nucleolar Sites Involved in rRNA Biogenesis. Mol. Cell. Biol. 24: 10894-10904 [Abstract] [Full Text]  
• Maraia, R. J. (2001). La Protein and the Trafficking of Nascent RNA Polymerase III Transcripts. J. Cell Biol. 153: F13-F18 [Abstract] [Full Text]  
• Maraia, R. J., Intine, R. V. A. (2001). Recognition of Nascent RNA by the Human La Antigen: Conserved and Divergent Features of Structure and Function. Mol. Cell. Biol. 21: 367-379 [Full Text]  
• Goodier, J. L., Maraia, R. J. (1998). Terminator-specific Recycling of a B1-Alu Transcription Complex by RNA Polymerase III Is Mediated by the RNA Terminus-binding Protein La. J. Biol. Chem. 273: 26110-26116 [Abstract] [Full Text]  
• Hsu, K., Chang, D.-Y., Maraia, R. J. (1995). Human Signal Recognition Particle (SRP) Alu-associated Protein Also Binds Alu Interspersed Repeat Sequence RNAs. J. Biol. Chem. 270: 10179-10186 [Abstract] [Full Text]