| Full text | |
| Author(s): |
da Silva, Marco Tulio A.
[1, 2]
;
Ambrosio, Daniela L.
[2]
;
Trevelin, Caroline C.
[2]
;
Watanabe, Tatiana F.
[2]
;
Laure, Helen J.
[3, 4]
;
Greene, Lewis J.
[3, 4]
;
Rosa, Jose C.
[3, 4]
;
Valentini, Sandro R.
[2]
;
Cicarelli, Regina M. B.
[2]
Total Authors: 9
|
| Affiliation: | [1] Univ Estadual Paulista, Inst Quim, Araraquara, SP - Brazil
[2] Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Ciencias Biol, Araraquara, SP - Brazil
[3] Univ Sao Paulo, Fac Med Ribeirao Preto, Ctr Quim Prot, Ribeirao Preto, SP - Brazil
[4] Univ Sao Paulo, Fac Med Ribeirao Preto, Ctr Reg Hemoterapia, Ribeirao Preto, SP - Brazil
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | Memórias do Instituto Oswaldo Cruz; v. 106, n. 2, p. 130-138, MAR 2011. |
| Web of Science Citations: | 4 |
| Abstract | |
Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems of trypanosomatids and other eukaryotes. In this context, certain small complexes of RNA and protein, which are named small nuclear ribonucleoproteins (U snRNPs), have an essential role in pre-mRNA processing, mainly during splicing. Even though they are well defined in mammals, snRNPs are still not well characterized in trypanosomatids. This study shows that a U5-15K protein is highly conserved among various trypanosomatid species. Tandem affinity pull-down assays revealed that this protein interacts with a novel U5-102K protein, which suggests the presence of a sub-complex that is potentially involved in the assembly of U4/U6-U5 tri-snRNPs. Functional analyses showed that U5-15K is essential for cell viability and is somehow involved with the trans and cis splicing machinery. Similar tandem affinity experiments with a trypanonosomatid U5-Cwc21 protein led to the purification of four U5 snRNP specific proteins and a Sm core, suggesting U5-Cwc-21 participation in the 35S U5 snRNP particle. Of these proteins, U5-200K was molecularly characterized. U5-200K has conserved domains, such as the DEAD/DEAH box helicase and Sec63 domains and displays a strong interaction with U5 snRNA. (AU) | |
| FAPESP's process: | 07/07476-0 - Fuctional and molecular characterization of Trypasomatids spliceosomal proteins |
| Grantee: | Regina Maria Barretto Cicarelli |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 06/05766-8 - Identification and functional characterization of U5 snRNP specific proteins in Trypanosoma cruzi |
| Grantee: | Regina Maria Barretto Cicarelli |
| Support Opportunities: | Regular Research Grants |