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Coelho Ribeiro Mde L, Espinosa J, Islam S, et al. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ. 2013;1:e2doi: 10.7717/peerj.2.
Coelho Ribeiro, M. d. e. . L., Espinosa, J., Islam, S., Martinez, O., Thanki, J. J., Mazariegos, S., Nguyen, T., Larina, M., Xue, B., & Uversky, V. N. (2013). Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ, 1e2. https://doi.org/10.7717/peerj.2
Coelho Ribeiro, Maria de Lourdes, et al. "Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome." PeerJ vol. 1 (2013): e2. doi: https://doi.org/10.7717/peerj.2
Coelho Ribeiro Mde L, Espinosa J, Islam S, Martinez O, Thanki JJ, Mazariegos S, Nguyen T, Larina M, Xue B, Uversky VN. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ. 2013 Feb 12;1:e2. doi: 10.7717/peerj.2. Print 2013. PMID: 23638354; PMCID: PMC3628832.
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PeerJ. 2013 Feb 12;1:e2. doi: 10.7717/peerj.2. Print 2013.

Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome.

PeerJ

Maria de Lourdes Coelho Ribeiro, Julio Espinosa, Sameen Islam, Osvaldo Martinez, Jayesh Jamnadas Thanki, Stephanie Mazariegos, Tam Nguyen, Maya Larina, Bin Xue, Vladimir N Uversky

Affiliations

  1. Cancer Imaging Metabolism, H. Lee Moffitt Cancer Center & Research Institute , United States ; Department of Molecular Medicine, University of South Florida , Tampa, Florida , United States.

PMID: 23638354 PMCID: PMC3628832 DOI: 10.7717/peerj.2

Abstract

Recent studies revealed that a significant fraction of any given proteome is presented by proteins that do not have unique 3D structures as a whole or in significant parts. These intrinsically disordered proteins possess dramatic structural and functional variability, being especially enriched in signaling and regulatory functions since their lack of fixed structure defines their ability to be involved in interaction with several proteins and allows them to be re-used in multiple pathways. Among recognized disorder-based protein functions are interactions with nucleic acids and multi-target binding; i.e., the functions ascribed to many spliceosomal proteins. Therefore, the spliceosome, a multimegadalton ribonucleoprotein machine catalyzing the excision of introns from eukaryotic pre-mRNAs, represents an attractive target for the focused analysis of the abundance and functionality of intrinsic disorder in its proteinaceous components. In yeast cells, spliceosome consists of five small nuclear RNAs (U1, U2, U4, U5, and U6) and a range of associated proteins. Some of these proteins constitute cores of the corresponding snRNA-protein complexes known as small nuclear ribonucleoproteins (snRNPs). Other spliceosomal proteins have various auxiliary functions. To gain better understanding of the functional roles of intrinsic disorder, we have studied the prevalence of intrinsically disordered proteins in the yeast spliceosome using a wide array of bioinformatics methods. Our study revealed that similar to the proteins associated with human spliceosomes (Korneta & Bujnicki, 2012), proteins found in the yeast spliceosome are enriched in intrinsic disorder.

Keywords: Intrinsic disorder; Intrinsically disordered protein; Protein function; Protein hub; Protein structure; Protein–RNA interaction; Protein–protein interaction; RNA–protein complex; Spliceosome; Splicing

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