Conserved structure of Snu13 from the highly reduced spliceosome of Cyanidioschyzon merolae
Autor: | Erin L. Garside, Andrew M. MacMillan, Stephen D. Rader, C. S. Black |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Genetics Spliceosome biology Functional analysis Sequence alignment Computational biology biology.organism_classification Biochemistry Yeast 03 medical and health sciences 030104 developmental biology Cyanidioschyzon merolae Minor spliceosome RNA splicing Molecular Biology Function (biology) |
Zdroj: | Protein Science. 25:911-916 |
ISSN: | 0961-8368 |
DOI: | 10.1002/pro.2894 |
Popis: | Structural and functional analysis of proteins involved in pre-mRNA splicing is challenging because of the complexity of the splicing machinery, known as the spliceosome. Bioinformatic, proteomic, and biochemical analyses have identified a minimal spliceosome in the red alga Cyanidioschyzon merolae. This spliceosome consists of only 40 core proteins, compared to ∼ 70 in S. cerevisiae (yeast) and ∼ 150 in humans. We report the X-ray crystallographic analysis of C. merolae Snu13 (CmSnu13), a key component of the assembling spliceosome, and present evidence for conservation of Snu13 function in this algal splicing pathway. The near identity of CmSnu13's three-dimensional structure to yeast and human Snu13 suggests that C. merolae should be an excellent model system for investigating the structure and function of the conserved core of the spliceosome. |
Databáze: | OpenAIRE |
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