Trypanosoma cruzi poly-zinc finger protein: A novel DNA/RNA-binding CCHC-zinc finger protein

A poly-zinc finger protein, designated PZFP1 was identified in Trypanosoma cruzi for the first time. The protein has 191 amino acids, contains seven motifs Cys(X)2Cys(X)4His(X)4Cys. A recombinant PZFP1 was generated in E. coli and the expected 21kDa polypeptide co-purified with two other inducible p...

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Detalles Bibliográficos
Autores principales: Espinosa, Joaquín Maximiliano, Portal, Daniel, Lobo, Guillermo Sebastián, Pereira, Claudio Alejandro, Alonso, Guillermo Daniel, Gómez, Eliana Beatriz, Flawiá, Mirtha María, Torres, Héctor Norberto
Publicado: 2003
Materias:
CCHC-type zinc finger
Poly-zinc finger protein
Serine-arginine-rich protein
TcPZFP1
TcSR
Trypanosoma cruzi
arginine
cell extract
double stranded DNA
oligonucleotide
protein
protein antibody
protozoal protein
recombinant protein
serine
zinc finger protein
amino acid sequence
article
cell nucleus
cellular distribution
cytoplasm
Escherichia coli
gel mobility shift assay
immunofluorescence
molecular recognition
molecular weight
nonhuman
nucleotide sequence
priority journal
protein analysis
protein DNA interaction
protein induction
protein localization
protein motif
protein protein interaction
protein purification
protein RNA binding
two hybrid system
Western blotting
yeast
Trypanosoma
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v131_n1_p35_Espinosa
http://hdl.handle.net/20.500.12110/paper_01666851_v131_n1_p35_Espinosa
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:A poly-zinc finger protein, designated PZFP1 was identified in Trypanosoma cruzi for the first time. The protein has 191 amino acids, contains seven motifs Cys(X)2Cys(X)4His(X)4Cys. A recombinant PZFP1 was generated in E. coli and the expected 21kDa polypeptide co-purified with two other inducible products of about 42 and 63kDa. Western blot analysis of cell extracts using an anti-PZFP1 antibody recognized a major band of 41kDa. Electrophoretic mobility shift analysis demonstrated that both, recombinant and native PZFP1, specifically interact with single-stranded DNA or RNA oligonucleotides carrying recognition sequences of other CCHC proteins. The protein was localized mainly in the cytoplasm and nucleus as observed by indirect immunofluorescence analysis. PZFP1 interacted specifically with a T. cruzi serine-arginine-rich protein (TcSR) in a yeast two-hybrid assay, suggesting a role in pre-mRNA processing. © 2003 Elsevier B.V. All rights reserved.

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