Characterization of intracellular RNase in heat processed yeast cells

Bueno, Gloria; Otero, Miguel; González, Arturo C.

doi:10.1007/bf00144314

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Cited by 4 publications

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“…In contrast, yeast cells possess only a mechanism of transcriptional control, and pre-existing mgNAs are rapidly degraded [5]. Moreover, heat stress of yeast cells leads to a reduction of the ribosome [6] and RNA content [71, and to an increase in ribonuclease activity [8]. Similar changes in the metabolism occur during the stationary growth phase when yeast cells suffer a lack of nutrition [9].…”

Section: Introductionmentioning

confidence: 99%

Induction of a proteinase by heat-shock in yeast

Gross

Schulz‐Harder

1986

FEMS Microbiology Letters

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In Saccharomyces cerevisiae heat‐shock induces an increase in proteinase activity. The induction is probably due to newly synthesized enzyme molecules, since the increase in proteinase activity can be inhibited by cycloheximide. Degradation of endogenous proteins is enhanced by EDTA, while the azocasein assay is not affected by MnCl2, MgCl2, or EDTA. The proteinase has a pH optimum of 8, and phenylmethylsulfonyl fluoride (PMSF) as well as chymostatin are strong inhibitors. We infer that the induced proteinase is probably identical with proteinase B of yeast.

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Section: Introductionmentioning

confidence: 99%