Stress response of yeast

Mager, Willem H.; Ferreira, Paulo Michel Pinheiro

doi:10.1042/bj2900001

Cited by 206 publications

(168 citation statements)

References 195 publications

(225 reference statements)

Supporting

Mentioning

160

Contrasting

Unclassified

Order By: Relevance

“…On the other hand, one of the heat shock proteins not induced during the adaptation to salt was Hsp83p, for which the 2D position is known and no increased synthesis was found (data not shown). The lack of Hsp83p induction is interesting because of the reported absolute involvement of the heat shock upstream element in the heat-induced expression of this gene (27). This involvement indicates that the salt-induced synthesis of some of the heat shock proteins was not solely a heat shock upstream elementdependent phenomenon and that some other regulatory mechanism acting during salt adaptation must be implemented for these genes.…”

Section: Discussionmentioning

confidence: 93%

Global changes in protein synthesis during adaptation of the yeast Saccharomyces cerevisiae to 0.7 M NaCl

Blomberg

1995

J Bacteriol

View full text Add to dashboard Cite

Exponentially growing Saccharomyces cerevisiae was challenged to increased salinity by transfer to 0.7 M NaCl medium, and changes in protein synthesis were examined during the 1st h of adaptation by use of two-dimensional gel electrophoresis coupled to computerized quantification. An impressive number of proteins displayed changes in the relative rate of synthesis, with most differences from nonstressed cells being found at between 20 and 40 min. During this period, 18 proteins exhibited more than eightfold increases in their rates of synthesis and were classified as highly NaCl responsive. Only two proteins were repressed to the same level. Most of these highly NaCl-responsive proteins seemed to constitute gene products not earlier reported to respond to dehydration. Applying a selection criterion to subsequent samples of a twofold change in the relative rate of synthesis, 14 different regulatory patterns were discerned. Most identified glycolytic enzymes exhibited a delayed response, and their rates of synthesis did not change until the middle phase of adaptation, with only a minor decrease in the rate of production. A slight salt-stimulated response was observed for some members of the HSP70 gene family. Overall, the data presented indicate complex intracellular signalling as well as involvement of diverse regulatory mechanisms during the period of adaptation to NaCl.

show abstract

Section: Discussionmentioning

confidence: 93%

Global changes in protein synthesis during adaptation of the yeast Saccharomyces cerevisiae to 0.7 M NaCl

Blomberg

1995

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…Strains subjected to a short period of stress or experiencing a constant stimulus of the stress response will display an enhanced viability upon exposure to a lethal temperature, reflecting an elevation of the intracellular concentration of heat shock proteins (Sanchez and Lindquist, 1990;Mager and Ferreira, 1993 ] enhanced tolerance to other forms of stress. In vivo, some components of the stress response machinery do confer tolerance to more than one form of stress.…”

Section: © European Molecular Biology Organizationmentioning

confidence: 99%

Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism

1999

View full text Add to dashboard Cite

“…The ∼70 kDa HSPs include constitutively expressed heat shock cognate 70 (HSC70) and stress-inducible HSP70. In normal, non-stressed conditions, intracellular HSPs play a critical role in the synthesis, transport and folding of proteins (Mager and Ferreira 1993;Morimoto 1993;Yura et al 1993). Amongst the HSP family, the HSP70s are the most evolutionarily conserved proteins and have been identified in a range of organisms, including molluscs (Kourtidis et al 2006a, b;Laursen et al 1997;Martynova et al 2007;Tirard et al 1995;Yoshino et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Larval excretory-secretory products from the parasite Schistosoma mansoni modulate HSP70 protein expression in defence cells of its snail host, Biomphalaria glabrata

Zahoor

Davies²,

Kirk³

et al. 2010

Cell Stress and Chaperones

View full text Add to dashboard Cite

Synthesis of heat shock proteins (HSPs) following cellular stress is a response shared by many organisms. Amongst the HSP family, the ∼70 kDa HSPs are the most evolutionarily conserved with intracellular chaperone and extracellular immunoregulatory functions. This study focused on the effects of larval excretory-secretory products (ESPs) from the parasite Schistosoma mansoni on HSP70 protein expression levels in haemocytes (defence cells) from its snail intermediate host Biomphalaria glabrata. S. mansoni larval stage ESPs are known to interfere with haemocyte physiology and behaviour. Haemocytes from two different B. glabrata strains, one which is susceptible to S. mansoni infection and one which is resistant, both showed reduced HSP70 protein levels following 1 h challenge with S. mansoni ESPs when compared to unchallenged controls; however, the reduction observed in the resistant strain was less marked. The decline in intracellular HSP70 protein persisted for at least 5 h in resistant snail haemocytes only. Furthermore, in schistosome-susceptible snails infected by S. mansoni for 35 days, haemocytes possessed approximately 70% less HSP70. The proteasome inhibitor, MG132, partially restored HSP70 protein levels in ESP-challenged haemocytes, demonstrating that the decrease in HSP70 was in part due to intracellular degradation. The extracellular signal-regulated kinase (ERK) signalling pathway appears to regulate HSP70 protein expression in these cells, as the mitogen-activated protein-ERK kinase 1/2 (MEK1/2) inhibitor, U0126, significantly reduced HSP70 protein levels. Disruption of intracellular HSP70 protein expression in B. glabrata haemocytes by S. mansoni ESPs may be a strategy employed by the parasite to manipulate the immune response of the intermediate snail host.

show abstract

Stress response of yeast

Cited by 206 publications

References 195 publications

Global changes in protein synthesis during adaptation of the yeast Saccharomyces cerevisiae to 0.7 M NaCl

Global changes in protein synthesis during adaptation of the yeast Saccharomyces cerevisiae to 0.7 M NaCl

Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism

Larval excretory-secretory products from the parasite Schistosoma mansoni modulate HSP70 protein expression in defence cells of its snail host, Biomphalaria glabrata

Contact Info

Product

Resources

About