The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae

Parvulins are a conserved group of peptidyl-prolyl cis/trans isomerases (PPIases) that catalyze the cis/trans isomerization of proline-preceding peptide bonds. Parvulin-class PPIases are structurally unrelated to cyclophilins and FK506-binding proteins that are defined as receptors for immunosuppres...

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Autor principal: Erben, Esteban Daniel
Publicado: 2007
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v153_n2_p186_Erben
http://hdl.handle.net/20.500.12110/paper_01666851_v153_n2_p186_Erben
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spelling paper:paper_01666851_v153_n2_p186_Erben2023-06-08T15:15:58Z The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae Erben, Esteban Daniel Cell cycle Parvulin Pin1 Prolyl cis/trans isomerization Trypanosoma cruzi Trypanosomatids amino acid derivative peptidylprolyl isomerase Pin1 protein parvulin Saccharomyces cerevisiae protein unclassified drug amino terminal sequence animal cell article catalysis cell structure gene mutation isomerization nonhuman phenotype priority journal protein analysis temperature Trypanosoma cruzi Western blotting Amino Acid Sequence Animals Cell Cycle Gene Expression Regulation Genetic Complementation Test Humans Molecular Sequence Data Peptidylprolyl Isomerase Protozoan Proteins Recombinant Proteins Sequence Alignment Sequence Analysis, DNA Trypanosoma cruzi Saccharomyces cerevisiae Trypanosoma cruzi Trypanosomatidae Parvulins are a conserved group of peptidyl-prolyl cis/trans isomerases (PPIases) that catalyze the cis/trans isomerization of proline-preceding peptide bonds. Parvulin-class PPIases are structurally unrelated to cyclophilins and FK506-binding proteins that are defined as receptors for immunosuppressive drugs. In Trypanosoma cruzi we identified parvulin TcPIN1 as a homolog of the human hPin1 PPIase. The 117 amino acids of the TcPIN1 display 40% identity with the catalytic core of hPin1 and exhibit prolyl cis/trans isomerase activity. TcPIN1 lacks the WW domain at the N-terminus, and is able to rescue the temperature-sensitive phenotype on a mutation in the Saccharomyces cerevisiae hPin1 homolog, ESS1/PTF1. Western blot analysis revealed that the enzyme was present both in dividing and non-dividing forms of T. cruzi. In epimastigote cells neither cell growth kinetics nor cell morphology was affected by the overexpression of the small parvulin TcPIN1. These results suggest the occurrence of a supplementary conserved level of post-translational control in trypanosomatids. © 2007 Elsevier B.V. All rights reserved. Fil:Erben, E.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v153_n2_p186_Erben http://hdl.handle.net/20.500.12110/paper_01666851_v153_n2_p186_Erben
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cell cycle
Parvulin
Pin1
Prolyl cis/trans isomerization
Trypanosoma cruzi
Trypanosomatids
amino acid derivative
peptidylprolyl isomerase Pin1
protein parvulin
Saccharomyces cerevisiae protein
unclassified drug
amino terminal sequence
animal cell
article
catalysis
cell structure
gene mutation
isomerization
nonhuman
phenotype
priority journal
protein analysis
temperature
Trypanosoma cruzi
Western blotting
Amino Acid Sequence
Animals
Cell Cycle
Gene Expression Regulation
Genetic Complementation Test
Humans
Molecular Sequence Data
Peptidylprolyl Isomerase
Protozoan Proteins
Recombinant Proteins
Sequence Alignment
Sequence Analysis, DNA
Trypanosoma cruzi
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosomatidae
spellingShingle Cell cycle
Parvulin
Pin1
Prolyl cis/trans isomerization
Trypanosoma cruzi
Trypanosomatids
amino acid derivative
peptidylprolyl isomerase Pin1
protein parvulin
Saccharomyces cerevisiae protein
unclassified drug
amino terminal sequence
animal cell
article
catalysis
cell structure
gene mutation
isomerization
nonhuman
phenotype
priority journal
protein analysis
temperature
Trypanosoma cruzi
Western blotting
Amino Acid Sequence
Animals
Cell Cycle
Gene Expression Regulation
Genetic Complementation Test
Humans
Molecular Sequence Data
Peptidylprolyl Isomerase
Protozoan Proteins
Recombinant Proteins
Sequence Alignment
Sequence Analysis, DNA
Trypanosoma cruzi
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosomatidae
Erben, Esteban Daniel
The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae
topic_facet Cell cycle
Parvulin
Pin1
Prolyl cis/trans isomerization
Trypanosoma cruzi
Trypanosomatids
amino acid derivative
peptidylprolyl isomerase Pin1
protein parvulin
Saccharomyces cerevisiae protein
unclassified drug
amino terminal sequence
animal cell
article
catalysis
cell structure
gene mutation
isomerization
nonhuman
phenotype
priority journal
protein analysis
temperature
Trypanosoma cruzi
Western blotting
Amino Acid Sequence
Animals
Cell Cycle
Gene Expression Regulation
Genetic Complementation Test
Humans
Molecular Sequence Data
Peptidylprolyl Isomerase
Protozoan Proteins
Recombinant Proteins
Sequence Alignment
Sequence Analysis, DNA
Trypanosoma cruzi
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosomatidae
description Parvulins are a conserved group of peptidyl-prolyl cis/trans isomerases (PPIases) that catalyze the cis/trans isomerization of proline-preceding peptide bonds. Parvulin-class PPIases are structurally unrelated to cyclophilins and FK506-binding proteins that are defined as receptors for immunosuppressive drugs. In Trypanosoma cruzi we identified parvulin TcPIN1 as a homolog of the human hPin1 PPIase. The 117 amino acids of the TcPIN1 display 40% identity with the catalytic core of hPin1 and exhibit prolyl cis/trans isomerase activity. TcPIN1 lacks the WW domain at the N-terminus, and is able to rescue the temperature-sensitive phenotype on a mutation in the Saccharomyces cerevisiae hPin1 homolog, ESS1/PTF1. Western blot analysis revealed that the enzyme was present both in dividing and non-dividing forms of T. cruzi. In epimastigote cells neither cell growth kinetics nor cell morphology was affected by the overexpression of the small parvulin TcPIN1. These results suggest the occurrence of a supplementary conserved level of post-translational control in trypanosomatids. © 2007 Elsevier B.V. All rights reserved.
author Erben, Esteban Daniel
author_facet Erben, Esteban Daniel
author_sort Erben, Esteban Daniel
title The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae
title_short The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae
title_full The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae
title_fullStr The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae
title_full_unstemmed The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae
title_sort trypanosoma cruzi pin1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ess1 in saccharomyces cerevisiae
publishDate 2007
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v153_n2_p186_Erben
http://hdl.handle.net/20.500.12110/paper_01666851_v153_n2_p186_Erben
work_keys_str_mv AT erbenestebandaniel thetrypanosomacruzipin1geneencodesaparvulinpeptidylprolylcistransisomeraseabletoreplacetheessentialess1insaccharomycescerevisiae
AT erbenestebandaniel trypanosomacruzipin1geneencodesaparvulinpeptidylprolylcistransisomeraseabletoreplacetheessentialess1insaccharomycescerevisiae
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