Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila.

Ingolia, Thomas D.; Slater, Michael; Craig, Elizabeth A.

doi:10.1128/mcb.2.11.1388

Cited by 172 publications

(115 citation statements)

References 35 publications

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“…SSB1 and SSB2 gene function has also been well characterised 14, 23, 29. Although SSB proteins display over 50% identity with SSA chaperones they are functionally distinct, as demonstrated by a series of experiments 27.…”

Section: Introductionmentioning

confidence: 98%

Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae

Jarnuczak¹,

Eyers

Schwartz³

et al. 2015

Proteomics

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Molecular chaperones play an important role in protein homeostasis and the cellular response to stress. In particular, the HSP70 chaperones in yeast mediate a large volume of protein folding through transient associations with their substrates. This chaperone interaction network can be disturbed by various perturbations, such as environmental stress or a gene deletion. Here, we consider deletions of two major chaperone proteins, SSA1 and SSB1, from the chaperone network in Sacchromyces cerevisiae. We employ a SILAC‐based approach to examine changes in global and local protein abundance and rationalise our results via network analysis and graph theoretical approaches. Although the deletions result in an overall increase in intracellular protein content, correlated with an increase in cell size, this is not matched by substantial changes in individual protein concentrations. Despite the phenotypic robustness to deletion of these major hub proteins, it cannot be simply explained by the presence of paralogues. Instead, network analysis and a theoretical consideration of folding workload suggest that the robustness to perturbation is a product of the overall network structure. This highlights how quantitative proteomics and systems modelling can be used to rationalise emergent network properties, and how the HSP70 system can accommodate the loss of major hubs.

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Section: Introductionmentioning

confidence: 98%

Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae

Jarnuczak¹,

Eyers

Schwartz³

et al. 2015

Proteomics

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confidence: 99%

“…The SSBI protein is 28% divergent from either of the yeast SSAI orSSA2 hsp70-related proteins and is 39% divergent from the Drosophila hsp70 protein (2,3). In contrast to the expression of the heat-induced SSAI gene, SSBI transcript levels decline upon heat shock (2,3,4). Limited sequence analysis of another heat shock cognate gene, SSB2 (formerly called YG103), shows less than 6% divergence in the amino tennini of the SSBI and SSB2 proteins, whereas the 5' non-protein coding regions are very dissimilar (3; L.S.…”

mentioning

confidence: 99%

“…The SSB1 gene (formerly called YG101) of Saccharomyces cerevisiae encodes a 66,601 molecular weight protein related to the hsp7O heat shock protein of other eucaryotes (1,2). The SSBI protein is 28% divergent from either of the yeast SSAI orSSA2 hsp70-related proteins and is 39% divergent from the Drosophila hsp70 protein (2,3).…”

mentioning

confidence: 99%

“…The 613 amino acid protein coding region for SSBI extends from nucleotide 210 to 2051 and the 5' end of the SSBI message maps to nucleotide 181 (± 5 bases) (2,4 …”

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confidence: 99%

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TheSSB1heat shock cognate gene of the yeastSaccharomyces cerevisiae

Slater

Craig

1989

Nucl Acids Res

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The SSB1 gene (formerly called YG101) of Saccharomyces cerevisiae encodes a 66,601 molecular weight protein related to the hsp7O heat shock protein of other eucaryotes (1,2). The SSBI protein is 28% divergent from either of the yeast SSAI orSSA2 hsp70-related proteins and is 39% divergent from the Drosophila hsp70 protein (2,3). In contrast to the expression of the heat-induced SSAI gene, SSBI transcript levels decline upon heat shock (2,3,4). Limited sequence analysis of another heat shock cognate gene, SSB2 (formerly called YG103), shows less than 6% divergence in the amino tennini of the SSBI and SSB2 proteins, whereas the 5' non-protein coding regions are very dissimilar (3; L.S. Stinson and E.A. Craig, unpublished data), suggesting a possible functional difference between SSBI and SSB2 proteins. A functional difference has also been postulated to explain a similar abrupt divergence in nonprotein coding regions between the SSAI and SSA2 genes (5). Interestingly, a ssbl ssb2 double mutant strain is cold-sensitive for growth (6) while a ssal ssa2 double mutant is heat-sensitive (7), indicating a functional difference between the SSA and SSB subfamilies of hsp70-related genes (1,6).The SSBI nucleotide sequence was determined on both DNA strands by the chemical cleavage method and all overlaps were obtained. The 613 amino acid protein coding region for SSBI extends from nucleotide 210 to 2051 and the 5' end of the SSBI message maps to nucleotide 181 (± 5 bases) (2,4).

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Thermal response ofHeterorhabditis bacteriophora transformed with theCaenorhabditis eleganshsp70 encoding gene

Hashmi

Glazer

et al. 1998

J. Exp. Zool.

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A heat‐shock response is induced when cells are exposed to temperatures slightly higher than their optimal physiological temperature. This response is based on the synthesis of heat‐shock proteins encoded by the heat‐shock genes. A correlation between the increased thermotolerance and production of 70‐kDa heat‐shock protein (hsp70) has been observed in many organisms. We tested this hypothesis by transferring a Caenorhabditis elegans heat‐inducible hsp70 A‐encoding gene into the entomopathogenic nematodes Heterorhabditis bacteriophora Hp88. Successful transformation of the gene was confirmed by Southern blot hybridization and polymerase chain reaction. Our blot studies showed that the transgenic nematodes contained five to ten copies per genome of the introduced hsp70 A gene. hsp70 mRNA transcripts were detected in both wild‐type and transgenic nematodes. Transcripts increased severalfold in transgenic nematodes upon heat shock. Infective juveniles of both transgenic and wild‐type nematodes that exposed to a sublethal heat treatment (35°C) for 2 h followed by a normally lethal heat treatment (40°C) for 1 h. More than 90% of transgenic nematodes survived heat treatment, compared to 2% to 3% of the wild‐type strain. Our observations establish that overexpression of hsp70 A gene resulted an enhanced thermotolerance in the transgenic nematodes. The transgenic nematodes displayed normal growth and development. J. Exp. Zool. 281:164–170, 1998. © 1998 Wiley‐Liss, Inc.

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Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila.

Cited by 172 publications

References 35 publications

Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae

Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae

TheSSB1heat shock cognate gene of the yeastSaccharomyces cerevisiae

Thermal response ofHeterorhabditis bacteriophora transformed with theCaenorhabditis eleganshsp70 encoding gene

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