| Grant number: | 17/11544-2 |
| Support Opportunities: | Scholarships in Brazil - Master |
| Start date: | October 01, 2017 |
| End date: | July 31, 2019 |
| Field of knowledge: | Biological Sciences - Biochemistry - Molecular Biology |
| Principal Investigator: | Carla Columbano de Oliveira |
| Grantee: | Thierry Pueblo Freitas Girotto |
| Host Institution: | Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil |
Abstract Splicing is the name given to the reaction of removal of introns in pre-RNAs and the binding of exons to former mature mRNAs. It is catalyzed by spliceosome, a highly dynamic complex formed by snRNPs, associations between snRNAs and proteins, facilitating the process of obtaining noncoding sections by means of two transesterification reactions.The spliceosome is not found in the cell as a preformed complex, on the contrary, it is assembled back into each pre-RNA that is processed. For this, an assembly is sequential and coordinated largely by protein interactions, such as which are dotted, often by post-translational modifications, such as phosphorylation, ubiquitination, sumoylation, among others, which may influence how protein functions, and Consequently in the splice step.An essential protein in Saccharomyces cerevisiae which plays a fundamentally seamless role is Cwc24, responsible for protecting the 5'SS (splicing site) from a premature nucleophilic attack during a first transesterification reaction, and which assists in stabilizing the binding of the U2 complex SnRNP to pre-RNA. Cwc24 interacts with several splicing machinery proteins: it was first isolated with Cef1, and was shown to interact with Prp8 and Brr2, as well as with Prp2 and Nop17. The Cwc24 protein has phosphorylation sites, which leads to believe that it undergoes modifications.The objective of this work is to analyze the role of phosphorylation in the interaction of Cwc24 with other spliceosome factors, evaluating which phosphorylation sites are essential for a function of this protein | |
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