Small nuclear ribonucleoprotein antigens are absent from 10S translation inhibitory ribonucleoprotein but present in cytoplasmic messenger ribonucleoprotein and polysomes |
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| Authors: | A M Boak S A Kovacs P F Agris D Chakraborty S Sarkar |
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| Affiliation: | 1. Department of Medicine and the Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211, USA;2. Department of Muscle Research, Boston Biomedical Research Institute Boston, Massachusetts 02114 USA;3. Department of Neurology, Harvard Medical School, Boston, Massachusetts 02114 USA;1. Genome Institute of Singapore, 60 Biopolis Street, Singapore 138672, Singapore;2. Cardiovascular Research Institute, National University of Singapore, Centre for Translational Medicine, 14 Medical Drive, Singapore 117599, Singapore;1. Institute of Biochemistry, Faculty of Biology and Chemistry (FB08), Justus-Liebig-University of Giessen, Heinrich-Buff-Ring 17, 35392 Giessen, Germany;2. Bioinformatics and Systems Biology, University of Giessen, Heinrich-Buff-Ring 58, 35392 Giessen, Germany;3. Institute for Virology, Faculty of Veterinary Medicine, University of Giessen, Schubertstr. 81, 35392 Giessen, Germany;1. State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China;2. CAS Center for Excellence in Biotic Interactions, University of Chinese Academy of Sciences, Beijing 100049, China;3. State Key Laboratory of Protein and Plant Gene Research, School of Advanced Agricultural Sciences, Peking University, Beijing 100871, China;4. State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, BIOPIC & ICG, and Center for Bioinformatics, Peking University, Beijing 100871, China;5. Department of Life Sciences, Henan Normal University, Xinxiang, Henan 453007, China;6. College of Life Sciences, Hebei University, Baoding, Hebei 071002, China;7. College of Life Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150038, China;8. Department of Ecology and Evolutionary Biology, University of Connecticut, 75 North Eagleville Road, Unit 3043, Storrs, CT 06269, USA;1. Institute of Biochemistry, University of Giessen, Giessen, Germany |
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| Abstract: | A cytoplasmic 10S ribonucleoprotein particle (iRNP), which is isolated from chick embryonic muscle, is a potent inhibitor of mRNA translation in vitro and contains a 4S translation inhibitory RNA species (iRNA). The iRNP particle shows similarity in size to the small nuclear ribonucleoprotein (snRNP) particles. Certain autoimmune disease patients contain antibodies directed against snRNP antigenic determinants. The possibility that iRNP may be related to the small nuclear particles was tested by immunoreactivity with monospecific autoimmune antibodies to six antigenic determinants (Sm, RNP, PM-1, SS-A (Ro), SS-B (La), and Scl-70). By Ouchterlony immunodiffusion assays, the cytoplasmic 10S iRNP did not show any immunoreactivity. Also, a more sensitive hemagglutination inhibition assay for detecting Sm and RNP antigens failed to show reactivity with the 10S iRNP. Thus, the 10S iRNP particles are distinct from the similarly sized snRNP. However, free and polysomal messenger ribonucleoprotein (mRNP) particles and polysomes also isolated from chick embryonic muscle and analyzed by Ouchterlony immunodiffusion and hemagglutination inhibition for the presence of the antigenic determinants showed reactivity to Sm and RNP autoantibodies, but were not antigenic for the other four antibodies. Some of the Sm antigenic peptides of mRNP particles and polysomes were identical to those purified from calf thymus nuclear extract, as judged by Western blot analysis. The association of Sm with free and polysomal mRNP and polysomes suggests that Sm may be involved in some cytoplasmic aspects of mRNA metabolism, in addition to a nuclear function in mRNA processing. |
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