Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/48394

TítuloThe sensitivity of the yeast, Saccharomyces cerevisiae, to acetic acid is influenced by DOM34 and RPL36A
Autor(es)Samanfar, Bahram
Shostak, Kristina
Moteshareie, Houman
Hajikarimlou, Maryam
Shaikho, Sarah
Omidi, Katayoun
Hooshyar, Mohsen
Burnside, Daniel
Galván Márquez, Imelda
Ludovico, Paula
Palavras-chaveYeast
Gene deletion
HSP
Protein expression
Saccharomyces cerevisiae
Acetic acid
Heat shock
DOM34 and RPL36A
DOM34
RPL36A
Data14-Nov-2017
EditoraPeerj, Inc.
RevistaPeerJ
Resumo(s)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.
TipoArtigo
URIhttps://hdl.handle.net/1822/48394
DOI10.7717/peerj.4037
ISSN2167-8359
e-ISSN2167-8359
Versão da editorahttps://peerj.com/
Arbitragem científicayes
AcessoAcesso aberto
Aparece nas coleções:ICVS - Artigos em revistas internacionais / Papers in international journals

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