The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30
In trypanosomes transcription is polycistronic and individual mRNAs are generated by a trans-splicing/polyadenylation coupled reaction. We identified a divergent trypanosome FIP1-like, a factor required for mRNA 3′ end formation from yeasts to human. Here we showed that it is a nuclear protein with...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v380_n4_p850_Bercovich http://hdl.handle.net/20.500.12110/paper_0006291X_v380_n4_p850_Bercovich |
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paper:paper_0006291X_v380_n4_p850_Bercovich2023-06-08T14:30:17Z The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 Bercovich, Natalia Vazquez, Martín Pablo Drug target mRNA processing Polyadenylation factors Protein interactions Trypanosome diseases amino acid cleavage and polyadenylation specificity factor cpsf30 protein fip1 protein nuclear protein protein unclassified drug amino acid blood level article cell surface controlled study human human cell nonhuman parasite viability polyadenylation priority journal protein interaction Trypanosoma Amino Acid Sequence Animals Cleavage And Polyadenylation Specificity Factor Molecular Sequence Data mRNA Cleavage and Polyadenylation Factors Polyadenylation Trypanosoma brucei brucei Trypanosoma cruzi Two-Hybrid System Techniques In trypanosomes transcription is polycistronic and individual mRNAs are generated by a trans-splicing/polyadenylation coupled reaction. We identified a divergent trypanosome FIP1-like, a factor required for mRNA 3′ end formation from yeasts to human. Here we showed that it is a nuclear protein with a speckled distribution essential for trypanosome viability. A strong interaction was found between TcFIP1-like and TcCPSF30, a component of the polyadenylation complex. We determined the specific amino acids in each protein involved in the interaction. Significant differences were found between the trypanosome interaction surface and its human counterpart. Although CPSF30/FIP1 interaction is known in other organisms, this is the first report mapping the interaction surface at the amino acid level. © 2009 Elsevier Inc. All rights reserved. Fil:Bercovich, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vazquez, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v380_n4_p850_Bercovich http://hdl.handle.net/20.500.12110/paper_0006291X_v380_n4_p850_Bercovich |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Drug target mRNA processing Polyadenylation factors Protein interactions Trypanosome diseases amino acid cleavage and polyadenylation specificity factor cpsf30 protein fip1 protein nuclear protein protein unclassified drug amino acid blood level article cell surface controlled study human human cell nonhuman parasite viability polyadenylation priority journal protein interaction Trypanosoma Amino Acid Sequence Animals Cleavage And Polyadenylation Specificity Factor Molecular Sequence Data mRNA Cleavage and Polyadenylation Factors Polyadenylation Trypanosoma brucei brucei Trypanosoma cruzi Two-Hybrid System Techniques |
spellingShingle |
Drug target mRNA processing Polyadenylation factors Protein interactions Trypanosome diseases amino acid cleavage and polyadenylation specificity factor cpsf30 protein fip1 protein nuclear protein protein unclassified drug amino acid blood level article cell surface controlled study human human cell nonhuman parasite viability polyadenylation priority journal protein interaction Trypanosoma Amino Acid Sequence Animals Cleavage And Polyadenylation Specificity Factor Molecular Sequence Data mRNA Cleavage and Polyadenylation Factors Polyadenylation Trypanosoma brucei brucei Trypanosoma cruzi Two-Hybrid System Techniques Bercovich, Natalia Vazquez, Martín Pablo The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 |
topic_facet |
Drug target mRNA processing Polyadenylation factors Protein interactions Trypanosome diseases amino acid cleavage and polyadenylation specificity factor cpsf30 protein fip1 protein nuclear protein protein unclassified drug amino acid blood level article cell surface controlled study human human cell nonhuman parasite viability polyadenylation priority journal protein interaction Trypanosoma Amino Acid Sequence Animals Cleavage And Polyadenylation Specificity Factor Molecular Sequence Data mRNA Cleavage and Polyadenylation Factors Polyadenylation Trypanosoma brucei brucei Trypanosoma cruzi Two-Hybrid System Techniques |
description |
In trypanosomes transcription is polycistronic and individual mRNAs are generated by a trans-splicing/polyadenylation coupled reaction. We identified a divergent trypanosome FIP1-like, a factor required for mRNA 3′ end formation from yeasts to human. Here we showed that it is a nuclear protein with a speckled distribution essential for trypanosome viability. A strong interaction was found between TcFIP1-like and TcCPSF30, a component of the polyadenylation complex. We determined the specific amino acids in each protein involved in the interaction. Significant differences were found between the trypanosome interaction surface and its human counterpart. Although CPSF30/FIP1 interaction is known in other organisms, this is the first report mapping the interaction surface at the amino acid level. © 2009 Elsevier Inc. All rights reserved. |
author |
Bercovich, Natalia Vazquez, Martín Pablo |
author_facet |
Bercovich, Natalia Vazquez, Martín Pablo |
author_sort |
Bercovich, Natalia |
title |
The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 |
title_short |
The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 |
title_full |
The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 |
title_fullStr |
The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 |
title_full_unstemmed |
The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30 |
title_sort |
fip-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with cpsf30 |
publishDate |
2009 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v380_n4_p850_Bercovich http://hdl.handle.net/20.500.12110/paper_0006291X_v380_n4_p850_Bercovich |
work_keys_str_mv |
AT bercovichnatalia thefip1likepolyadenylationfactorintrypanosomesandthestructuralbasisforitsinteractionwithcpsf30 AT vazquezmartinpablo thefip1likepolyadenylationfactorintrypanosomesandthestructuralbasisforitsinteractionwithcpsf30 AT bercovichnatalia fip1likepolyadenylationfactorintrypanosomesandthestructuralbasisforitsinteractionwithcpsf30 AT vazquezmartinpablo fip1likepolyadenylationfactorintrypanosomesandthestructuralbasisforitsinteractionwithcpsf30 |
_version_ |
1768544530507759616 |