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The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process

BACKGROUND: The gene YCL047C, which has been renamed promoter of filamentation gene (POF1), has recently been described as a cell component involved in yeast filamentous growth. The objective of this work is to understand the molecular and biological function of this gene. RESULTS: Here, we report t...

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Autores principales: Costa, Iris M, Nasser, Tallybia HT, Demasi, Marilene, Nascimento, Rafaella MP, Netto, Luis ES, Miyamoto, Sayuri, Prado, Fernanda M, Monteiro, Gisele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3282682/
https://www.ncbi.nlm.nih.gov/pubmed/22204397
http://dx.doi.org/10.1186/1471-2180-11-268
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author Costa, Iris M
Nasser, Tallybia HT
Demasi, Marilene
Nascimento, Rafaella MP
Netto, Luis ES
Miyamoto, Sayuri
Prado, Fernanda M
Monteiro, Gisele
author_facet Costa, Iris M
Nasser, Tallybia HT
Demasi, Marilene
Nascimento, Rafaella MP
Netto, Luis ES
Miyamoto, Sayuri
Prado, Fernanda M
Monteiro, Gisele
author_sort Costa, Iris M
collection PubMed
description BACKGROUND: The gene YCL047C, which has been renamed promoter of filamentation gene (POF1), has recently been described as a cell component involved in yeast filamentous growth. The objective of this work is to understand the molecular and biological function of this gene. RESULTS: Here, we report that the protein encoded by the POF1 gene, Pof1p, is an ATPase that may be part of the Saccharomyces cerevisiae protein quality control pathway. According to the results, Δpof1 cells showed increased sensitivity to hydrogen peroxide, tert-butyl hydroperoxide, heat shock and protein unfolding agents, such as dithiothreitol and tunicamycin. Besides, the overexpression of POF1 suppressed the sensitivity of Δpct1, a strain that lacks a gene that encodes a phosphocholine cytidylyltransferase, to heat shock. In vitro analysis showed, however, that the purified Pof1p enzyme had no cytidylyltransferase activity but does have ATPase activity, with catalytic efficiency comparable to other ATPases involved in endoplasmic reticulum-associated degradation of proteins (ERAD). Supporting these findings, co-immunoprecipitation experiments showed a physical interaction between Pof1p and Ubc7p (an ubiquitin conjugating enzyme) in vivo. CONCLUSIONS: Taken together, the results strongly suggest that the biological function of Pof1p is related to the regulation of protein degradation.
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spelling pubmed-32826822012-02-21 The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process Costa, Iris M Nasser, Tallybia HT Demasi, Marilene Nascimento, Rafaella MP Netto, Luis ES Miyamoto, Sayuri Prado, Fernanda M Monteiro, Gisele BMC Microbiol Research Article BACKGROUND: The gene YCL047C, which has been renamed promoter of filamentation gene (POF1), has recently been described as a cell component involved in yeast filamentous growth. The objective of this work is to understand the molecular and biological function of this gene. RESULTS: Here, we report that the protein encoded by the POF1 gene, Pof1p, is an ATPase that may be part of the Saccharomyces cerevisiae protein quality control pathway. According to the results, Δpof1 cells showed increased sensitivity to hydrogen peroxide, tert-butyl hydroperoxide, heat shock and protein unfolding agents, such as dithiothreitol and tunicamycin. Besides, the overexpression of POF1 suppressed the sensitivity of Δpct1, a strain that lacks a gene that encodes a phosphocholine cytidylyltransferase, to heat shock. In vitro analysis showed, however, that the purified Pof1p enzyme had no cytidylyltransferase activity but does have ATPase activity, with catalytic efficiency comparable to other ATPases involved in endoplasmic reticulum-associated degradation of proteins (ERAD). Supporting these findings, co-immunoprecipitation experiments showed a physical interaction between Pof1p and Ubc7p (an ubiquitin conjugating enzyme) in vivo. CONCLUSIONS: Taken together, the results strongly suggest that the biological function of Pof1p is related to the regulation of protein degradation. BioMed Central 2011-12-28 /pmc/articles/PMC3282682/ /pubmed/22204397 http://dx.doi.org/10.1186/1471-2180-11-268 Text en Copyright ©2011 Costa et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Costa, Iris M
Nasser, Tallybia HT
Demasi, Marilene
Nascimento, Rafaella MP
Netto, Luis ES
Miyamoto, Sayuri
Prado, Fernanda M
Monteiro, Gisele
The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
title The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
title_full The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
title_fullStr The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
title_full_unstemmed The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
title_short The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process
title_sort promoter of filamentation (pof1) protein from saccharomyces cerevisiae is an atpase involved in the protein quality control process
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3282682/
https://www.ncbi.nlm.nih.gov/pubmed/22204397
http://dx.doi.org/10.1186/1471-2180-11-268
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