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The sensitivity of the yeast, Saccharomyces cerevisiae, to acetic acid is influenced by DOM34 and RPL36A

Authors :
Bahram Samanfar
Kristina Shostak
Houman Moteshareie
Maryam Hajikarimlou
Sarah Shaikho
Katayoun Omidi
Mohsen Hooshyar
Daniel Burnside
Imelda Galván Márquez
Tom Kazmirchuk
Thet Naing
Paula Ludovico
Anna York-Lyon
Kama Szereszewski
Cindy Leung
Jennifer Yixin Jin
Rami Megarbane
Myron L. Smith
Mohan Babu
Martin Holcik
Ashkan Golshani
Source :
PeerJ, Vol 5, p e4037 (2017)
Publication Year :
2017
Publisher :
PeerJ Inc., 2017.

Abstract

The presence of acetic acid during industrial alcohol fermentation reduces the yield of fermentation by imposing additional stress on the yeast cells. The biology of cellular responses to stress has been a subject of vigorous investigations. Although much has been learned, details of some of these responses remain poorly understood. Members of heat shock chaperone HSP proteins have been linked to acetic acid and heat shock stress responses in yeast. Both acetic acid and heat shock have been identified to trigger different cellular responses including reduction of global protein synthesis and induction of programmed cell death. Yeast HSC82 and HSP82 code for two important heat shock proteins that together account for 1–2% of total cellular proteins. Both proteins have been linked to responses to acetic acid and heat shock. In contrast to the overall rate of protein synthesis which is reduced, the expression of HSC82 and HSP82 is induced in response to acetic acid stress. In the current study we identified two yeast genes DOM34 and RPL36A that are linked to acetic acid and heat shock sensitivity. We investigated the influence of these genes on the expression of HSP proteins. Our observations suggest that Dom34 and RPL36A influence translation in a CAP-independent manner.

Details

Language :
English
ISSN :
21678359
Volume :
5
Database :
Directory of Open Access Journals
Journal :
PeerJ
Publication Type :
Academic Journal
Accession number :
edsdoj.6abdc1c3312d4ec3bc2b658072716102
Document Type :
article
Full Text :
https://doi.org/10.7717/peerj.4037