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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2007
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 13250caa a22014057a 4500 | ||
|---|---|---|---|
| 001 | PAPER-6573 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203616.0 | ||
| 008 | 190411s2007 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-34247515664 | |
| 024 | 7 | |2 Molecular Sequence Numbers |a GENBANK: DQ303420, DQ420359; | |
| 024 | 7 | |2 cas |a NIMA-interacting peptidylprolyl isomerase; Peptidylprolyl Isomerase, 5.2.1.8; Protozoan Proteins; Recombinant Proteins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a MBIPD | ||
| 100 | 1 | |a Erben, E.D. | |
| 245 | 1 | 4 | |a The Trypanosoma cruzi PIN1 gene encodes a parvulin peptidyl-prolyl cis/trans isomerase able to replace the essential ESS1 in Saccharomyces cerevisiae |
| 260 | |c 2007 | ||
| 270 | 1 | 0 | |m Téllez-Iñón, M.T.; Instituto de Investigaciones en Ingenieria Genetica y Biologia Molecular (INGEBI-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina; email: mtellez@dna.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a 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. |l eng | |
| 536 | |a Detalles de la financiación: National Research Council | ||
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica | ||
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: This work was supported by grants from the Agencia Nacional de Promoción Científica y Tecnológica (ANPCYT), the National Research Council (CONICET) and the Universidad de Buenos Aires to MTTI. We are indebted to Dr. Berta F. de Cazzulo and Dr. Claudio Pereira for providing amastigote and trypomastigote cultures. We are grateful to Dr. G. Fischer for helpful support. Also we thank Steven D. Hanes (Wadsworth Center) for the yeast plasmids and strains. EE is a Doctoral Fellow of ANPCYT; MTTI is a Career Investigator of CONICET. | ||
| 593 | |a Instituto de Investigaciones en Ingenieria Genetica y Biologia Molecular (INGEBI-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina | ||
| 593 | |a Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle, Germany | ||
| 690 | 1 | 0 | |a CELL CYCLE |
| 690 | 1 | 0 | |a PARVULIN |
| 690 | 1 | 0 | |a PIN1 |
| 690 | 1 | 0 | |a PROLYL CIS/TRANS ISOMERIZATION |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a TRYPANOSOMATIDS |
| 690 | 1 | 0 | |a AMINO ACID DERIVATIVE |
| 690 | 1 | 0 | |a PEPTIDYLPROLYL ISOMERASE PIN1 |
| 690 | 1 | 0 | |a PROTEIN PARVULIN |
| 690 | 1 | 0 | |a SACCHAROMYCES CEREVISIAE PROTEIN |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a AMINO TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a ANIMAL CELL |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CATALYSIS |
| 690 | 1 | 0 | |a CELL STRUCTURE |
| 690 | 1 | 0 | |a GENE MUTATION |
| 690 | 1 | 0 | |a ISOMERIZATION |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PHENOTYPE |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN ANALYSIS |
| 690 | 1 | 0 | |a TEMPERATURE |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a WESTERN BLOTTING |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a CELL CYCLE |
| 690 | 1 | 0 | |a GENE EXPRESSION REGULATION |
| 690 | 1 | 0 | |a GENETIC COMPLEMENTATION TEST |
| 690 | 1 | 0 | |a HUMANS |
| 690 | 1 | 0 | |a MOLECULAR SEQUENCE DATA |
| 690 | 1 | 0 | |a PEPTIDYLPROLYL ISOMERASE |
| 690 | 1 | 0 | |a PROTOZOAN PROTEINS |
| 690 | 1 | 0 | |a RECOMBINANT PROTEINS |
| 690 | 1 | 0 | |a SEQUENCE ALIGNMENT |
| 690 | 1 | 0 | |a SEQUENCE ANALYSIS, DNA |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a SACCHAROMYCES CEREVISIAE |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a TRYPANOSOMATIDAE |
| 700 | 1 | |a Daum, S. | |
| 700 | 1 | |a Téllez-Iñón, M.T. | |
| 773 | 0 | |d 2007 |g v. 153 |h pp. 186-193 |k n. 2 |p Mol. Biochem. Parasitol. |x 01666851 |w (AR-BaUEN)CENRE-6136 |t Molecular and Biochemical Parasitology | |
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