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spelling 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
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