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

BMC Microbiology

Research Article

Fernanda M Prado¹  Sayuri Miyamoto¹  Rafaella MP Nascimento²  Luis ES Netto²  Tallybia HT Nasser³  Gisele Monteiro³  Iris M Costa³  Marilene Demasi⁴ 

[1] Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo - USP, São Paulo-SP, Brazil;Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo - USP, São Paulo-SP, Brazil;Departamento de Tecnologia Bioquímico-Farmacêutica, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo - USP, São Paulo-SP, Brazil;Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo-SP, Brazil;

关键词: unfolded protein response;    endoplasmic reticulum stress;    antioxidant response;   

DOI  :  10.1186/1471-2180-11-268

 received in 2011-08-31, accepted in 2011-12-28,  发布年份 2011

来源: Springer

【 摘 要 】

BackgroundThe 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.ResultsHere, 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.ConclusionsTaken together, the results strongly suggest that the biological function of Pof1p is related to the regulation of protein degradation.

【 授权许可】

Unknown   
© Costa et al; licensee BioMed Central Ltd. 2011. This article is published under license to BioMed Central Ltd. 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.