Erratum to: Sequence of a 4.8 kb fragment of <i>Saccharomyces cerevisiae</i> chromosome II including three essential open reading frames

Baur, Axel; Schaaff-Gerstenschläger, Ine; Boles, Eckhard; Miosga, Thomas; Rose, Matthias; Zimmermann, Friedrich K.

doi:10.1002/yea.320100113

Cited by 7 publications

(9 citation statements)

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“…In contrast, Cns1 is essential at all temperatures (2). Moreover, the lethality caused by the cns1⌬ mutation cannot be suppressed by overexpression of other TPR-containing proteins, including Cpr6, Cpr7, or Sti1.…”

Section: Discussionmentioning

confidence: 95%

Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7ΔCells

Marsh

Kalton

Gaber

1998

Molecular and Cellular Biology

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Saccharomyces cerevisiae harbors two cyclophilin 40-type enzymes, Cpr6 and Cpr7, which are components of the Hsp90 molecular chaperone machinery. Cpr7 is required for normal growth and is required for maximal activity of heterologous Hsp90-dependent substrates, including glucocorticoid receptor (GR) and the oncogenic tyrosine kinase pp60 v-src . In addition, it has recently been shown that Cpr7 plays a major role in negative regulation of the S. cerevisiae heat shock transcription factor (HSF). To better understand functions associated with Cpr7, a search was undertaken for multicopy suppressors of the cpr7⌬ slow-growth phenotype. The screen identified a single gene, designated CNS1 (for cyclophilin seven suppressor), capable of suppressing the cpr7⌬ growth defect. Overexpression of CNS1 in cpr7⌬ cells also largely restored GR activity and negative regulation of HSF. In vitro protein retention experiments in which Hsp90 heterocomplexes were precipitated resulted in coprecipitation of Cns1. Interaction between Cns1 and the carboxy terminus of Hsp90 was also shown by two-hybrid analysis. The functional consequences of CNS1 overexpression and its physical association with the Hsp90 machinery indicate that Cns1 is a previously unidentified component of molecular chaperone complexes. Thus far, Cns1 is the only tetratricopeptide repeat-containing component of Hsp90 heterocomplexes found to be essential for cell viability under all conditions tested.Cells rely on molecular chaperones to facilitate the folding of nascent polypeptides, prevent protein aggregation, and enable proper inter-and intramolecular interactions. Indispensable in both Saccharomyces cerevisiae (5) and Drosophila melanogaster (13), Hsp90 is one of the most abundant and highly conserved chaperones. In vitro, Hsp90 displays general chaperone properties by preventing the aggregation of proteins such as citrate synthase (52) and casein kinase II (30) and by maintaining ␤-galactosidase (21) in a folding-competent state. In vivo, however, Hsp90 is not required for the folding of most proteins (33) but instead plays a key role in the maturation of a small subset of proteins typically involved in signal transduction (3,32,42). It is needed for the maturation of certain steroid hormone receptors (40,43,44), basic helix-loop-helix transcription factors (45

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Section: Discussionmentioning

confidence: 95%

Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7ΔCells

Marsh

Kalton

Gaber

1998

Molecular and Cellular Biology

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“…A physical interaction between Cns1 und Hsp90 was shown by immunoprecipitation (23). Cns1 is a protein of 385 amino acids, resulting in a molecular mass of 44.1 kDa (24). The threedimensional structure of Cns1 is still unknown.…”

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confidence: 99%

Cns1 Is an Activator of the Ssa1 ATPase Activity

Hainzl¹,

Wegele²,

Richter

et al. 2004

Journal of Biological Chemistry

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Hsp90 is a key mediator in the folding process of a growing number of client proteins. The molecular chaperone cooperates with many co-chaperones and partner proteins to fulfill its task. In Saccharomyces cerevisiae, several co-chaperones of Hsp90 interact with Hsp90 via a tetratricopeptide repeat (TPR) domain. Here we show that one of these proteins, Cns1, binds both to Hsp90 and to the yeast Hsp70 protein Ssa1 with comparable affinities. This is reminiscent of Sti1, another TPR-containing co-chaperone. Unlike Sti1, Cns1 exhibits no influence on the ATPase of Hsp90. However, it activates the ATPase of Ssa1 up to 30-fold by accelerating the ratelimiting ATP hydrolysis step. This stimulating effect is mediated by the N-terminal TPR-containing part of Cns1, whereas the C-terminal part showed no effect. Competition experiments allow the conclusion that Hsp90 and Ssa1 compete for binding to the single TPR domain of Cns1. Taken together, Cns1 is a potent cochaperone of Ssa1. Our findings highlight the importance of the regulation of Hsp70 function in the context of the Hsp90 chaperone cycle.

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“…The RIB1 protein sequence from P. guilliermondii shows a remarkable degree of homology to a putative GTP-cyclohydrolase from S. cerevisiae (Doignon et a]., 1993;Baur et al, 1993), with 60% identical amino acids and more than 70% overall homology over the entire length of the protein.…”

Section: Ctt Leumentioning

confidence: 99%

“…GTP-cyclohydrolase ( R I B I ) catalyses the initial and rate-limiting step of riboflavin synthesis and is subject to multiple metabolic controls. Properties of GTP-cyclohydrolases I1 of Escherichia coli and Bacillus subtilis were thoroughly studied and structural genes coding for these proteins were cloned and sequenced (Foor and Brown, 1975;Mironov et al, 1989;Boretskii et al, 1991Boretskii et al, , 1992Richter et al, 1993). The yeast Pichia guilliermondii is of great industrial interest because of its high capacity to synthesize riboflavin.…”

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confidence: 99%

Molecular cloning of the GTP‐cyclohydrolase structural gene RIB1 of Pichia guilliermondii involved in riboflavin biosynthesis

Liauta-Teglivets

Hasslacher

Boretskiĭ

et al. 1995

Yeast

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The structural gene of GTP-cyclohydrolase, involved in riboflavin biosynthesis, was cloned from a Pichia guilliermondii genomic library. A 1855 bp genomic DNA fragment complementing the riboflavin auxotrophies of an Escherichia coli ribA mutant, defective in GTP-cyclohydrolase II, and a P. guilliermondii rib1 mutant was isolated and sequenced. An open reading frame with the potential to encode a protein of 344 amino acids with a predicted molecular mass of 38,711 Da was detected. The P. guilliermondii enzyme shows a high degree of homology to GTP-cyclohydrolases type II from E. coli and Baccillus subtilis and to GTP-cyclohydrolase from Saccharomyces cerevisiae. Functional GTP-cyclohydrolase from P. guilliermondii may consist of four identical subunits.

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Erratum to: Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II including three essential open reading frames

Cited by 7 publications

References 0 publications

Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7ΔCells

Cns1 Is an Essential Protein Associated with the Hsp90 Chaperone Complex in Saccharomyces cerevisiae That Can Restore Cyclophilin 40-Dependent Functions in cpr7ΔCells

Cns1 Is an Activator of the Ssa1 ATPase Activity

Molecular cloning of the GTP‐cyclohydrolase structural gene RIB1 of Pichia guilliermondii involved in riboflavin biosynthesis

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