Journal article

Publication year: 1991

Pages: 9097-9101

Journal: Proceedings of the National Academy of Sciences

Volume number: 88

Issue number: 20

ISSN: 0027-8424

eISSN: 1091-6490

DOI Link: https://doi.org/10.1073/pnas.88.20.9097

Publisher: National Academy of Sciences

Abstract: 
We have developed a procedure for the affinity purification of small nuclear ribonucleoproteins (snRNPs) of Trypanosoma brucei (U2 and U4/U6 snRNPs), which are essential for trans splicing. Each of these snRNPs can be specifically and efficiently selected from T. brucei extracts through biotinylated antisense 2'-O-methylated RNA oligonucleotides immobilized on streptavidin-agarose. Protein analysis revealed a set of five low molecular weight polypeptides common to the U2 and U4/U6 snRNPs and the spliced leader RNP. In addition, several U2 and U4/U6 snRNP-specific protein components were identified. Using monoclonal antibodies against human snRNP proteins, we could not detect any significant cross-reaction with the trypanosomal U2 snRNP proteins. Thus, the trypanosomal snRNPs exhibit principal differences from the higher eukaryotic snRNPs not only in their RNA but also in their protein components.

Harvard Citation style: Palfi, Z., Günzl, A., Cross, M. and Bindereif, A. (1991) Affinity purification of Trypanosoma brucei small nuclear ribonucleoproteins reveals common and specific protein components., Proceedings of the National Academy of Sciences, 88(20), pp. 9097-9101. https://doi.org/10.1073/pnas.88.20.9097

APA Citation style: Palfi, Z., Günzl, A., Cross, M., & Bindereif, A. (1991). Affinity purification of Trypanosoma brucei small nuclear ribonucleoproteins reveals common and specific protein components.. Proceedings of the National Academy of Sciences. 88(20), 9097-9101. https://doi.org/10.1073/pnas.88.20.9097