Disease relevance of HSP30

• In addition ethanol (6-8%) causes the same two major changes to integral plasma-membrane protein composition that result from a sublethal heat stress, reduction in levels of the plasma membrane ATPase protein and acquisition of the plasma membrane heat-shock protein Hsp30 [1].

High impact information on HSP30

• Furthermore, DNA microarray analysis of BTN1 and btn1-delta strains revealed differential expression of two genes, with at least one, HSP30, involved in pH control [2].
• Moreover, a novel War1p- and Msn2p/4p-independent regulon that includes HSP30 was identified [3].
• This study has also revealed unexpected links between mitochondria and remote metabolic pathways since frataxin deficiency also enhances the expression of genes such as HSP30, that escape to AFT1 control [4].
• Two main target genes of Haa1 are the multidrug resistance gene YGR138c and the YRO2 homolog to the plasma membrane Hsp30 [5].
• The yeast model for batten disease: mutations in BTN1, BTN2, and HSP30 alter pH homeostasis [6].

Biological context of HSP30

• We showed that the HSP30 promoter can induce high gene expression during late stationary phase and remains active until the end of the wine fermentation process [7].
• One ORF showed considerable homology (46%) to a hypothetical chromosome III gene; another, putatively very hydrophobic gene product, was 30% identical to the heat-shock protein HSP30 [8].
• Mutation of the Thr-912 residue within the C-terminal domain of H+-ATPase, a potential site of phosphorylation by the Ca2+-calmodulin-dependent protein kinase, also abolishes any effect of Hsp30 [9].
• Through in vivo pulse-labelling of plasma membrane proteins synthesised before and during heat shock, followed by subcellular fractionation, it was shown that hsp30 is the only protein induced by the yeast heat-shock response that substantially copurifies with plasma membranes [10].
• Consistent with the role of Hsp30 being energy conservation, Hsp30 null cultures give lower final biomass yields [11].

Anatomical context of HSP30

• HSP30, encoding the plasma membrane heat shock protein, is shown in this study to be activated by several stresses [12].

Associations of HSP30 with chemical compounds

• Thus, the HSP26 and the HSP30 promoter can be used for late, phase-specific expression of the desired genes with glucose or maltose as carbon source, and HSP12 with glucose only [13].
• They also have lower ATP levels, consistent with higher H(+)-ATPase activity, at the glucose exhaustion stage of batch fermentations (diauxic lag), when Hsp30 is normally induced [11].
• This Hsp30 is induced by several stresses, including heat shock, ethanol exposure, severe osmostress, weak organic acid exposure and glucose limitation [11].

Other interactions of HSP30

• HSP12, HSP26 and HSP30 were highly expressed [13].
• In this study, we analyzed the in vivo binding of yeast heat shock factor (HSF) to the promoters of target genes ScSSA1, ScSSA4, HSP30 and HSP104, using chromatin immunoprecipitation [14].
• The HSP30 promoter has no good agreement to the HSE consensus and its stress activation is unaffected by a mutation (hsf1-m3) that causes defective heat shock activation of Hsf1-dependent genes [12].
• We refer to YDR033w as MRH1 to denote that it encodes a membrane protein related to Hsp30p [15].

References