Repetitive Dictyostelium heat-shock promotor functions in Saccharomyces cerevisiae.

The Dictyostelium genome contains 40 copies of a 4.7-kilobase repetitive and apparently transposable DNA sequence (DIRS-1) and about 250 smaller elements that appear to be deletions or rearrangements of DIRS-1. Transcripts of these sequences are induced during differentiation and also by heat shock treatment of growing cells. We showed that one such cloned element, pB41.6 (2.5 kilobases) contains a nucleotide sequence identical to the Drosophila consensus heat shock promotor. To test whether this sequence might indeed control the expression of DIRS-1-related RNAs, we have cloned this genomic segment into yeast cells. In yeast cells, 41.6 directs synthesis of a 1.7-kilobase RNA that is induced at least 10-fold by heat shock. Transcription initiates at about 124 bases 3' of the putative promotor sequence and terminates within the 41.6 insert. A 381-base-pair subclone that contains the putative promotor sequence is sufficient to induce the heat shock response of 41.6 in yeast cells.

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DNA damage and heat shock dually regulate genes in Saccharomyces cerevisiae.

Molecular and Cellular Biology ◽

10.1128/mcb.6.1.90 ◽

1986 ◽

Vol 6 (1) ◽

pp. 90-96 ◽

Cited By ~ 39

Author(s):

T McClanahan ◽

K McEntee

Keyword(s):

Saccharomyces Cerevisiae ◽

Dna Damage ◽

Heat Shock ◽

Shock Treatment ◽

Northern Hybridization ◽

Heat Shock Treatment ◽

Base Pairs ◽

S1 Nuclease ◽

Hsp70 Family ◽

Transcriptional Start Sites

Two Saccharomyces cerevisiae genes isolated in a differential hybridization screening for DNA damage regulation (DDR genes) were also transcriptionally regulated by heat shock treatment. A 0.45-kilobase transcript homologous to the DDRA2 gene and a 1.25-kilobase transcript homologous to the DDR48 gene accumulated after exposure of cells to 4-nitroquinoline-1-oxide (NQO; 1 to 1.5 microgram/ml) or brief heat shock (20 min at 37 degrees C). The DDRA2 transcript, which was undetectable in untreated cells, was induced to high levels by these treatments, and the DDR48 transcript increased more than 10-fold as demonstrated by Northern hybridization analysis. Two findings argue that dual regulation of stress-responsive genes is not common in S. cerevisiae. First, two members of the heat shock-inducible hsp70 family of S. cerevisiae, YG100 and YG102, were not induced by exposure to NQO. Second, at least one other DNA-damage-inducible gene, DIN1, was not regulated by heat shock treatment. We examined the structure of the induced RNA homologous to DDRA2 after heat shock and NQO treatments by S1 nuclease protection experiments. Our results demonstrated that the DDRA2 transcript initiates equally frequently at two sites separated by 5 base pairs. Both transcriptional start sites were utilized when cells were exposed to either NQO or heat shock treatment. These results indicate that DDRA2 and DDR48 are members of a unique dually regulated stress-responsive family of genes in S. cerevisiae.

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Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae

Molecular and Cellular Biology ◽

10.1128/mcb.11.2.1062-1068.1991 ◽

1991 ◽

Vol 11 (2) ◽

pp. 1062-1068

Author(s):

H J Yost ◽

S Lindquist

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Synthesis ◽

Heat Shock ◽

Heat Shock Proteins ◽

Heat Shock Response ◽

Rna Splicing ◽

Yeast Cells ◽

Yeast Saccharomyces Cerevisiae ◽

Shock Response ◽

Shock Proteins

In the yeast Saccharomyces cerevisiae, the splicing of mRNA precursors is disrupted by a severe heat shock. Mild heat treatments prior to severe heat shock protect splicing from disruption, as was previously reported for Drosophila melanogaster. In contrast to D. melanogaster, protein synthesis during the pretreatment is not required to protect splicing in yeast cells. However, protein synthesis is required for the rapid recovery of splicing once it has been disrupted by a sudden severe heat shock. Mutations in two classes of yeast hsp genes affect the pattern of RNA splicing during the heat shock response. First, certain hsp70 mutants, which overproduce other heat shock proteins at normal temperatures, show constitutive protection of splicing at high temperatures and do not require pretreatment. Second, in hsp104 mutants, the recovery of RNA splicing after a severe heat shock is delayed compared with wild-type cells. These results indicate a greater degree of specialization in the protective functions of hsps than has previously been suspected. Some of the proteins (e.g., members of the hsp70 and hsp82 gene families) help to maintain normal cellular processes at higher temperatures. The particular function of hsp104, at least in splicing, is to facilitate recovery of the process once it has been disrupted.

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DNA damage and heat shock dually regulate genes in Saccharomyces cerevisiae

Molecular and Cellular Biology ◽

10.1128/mcb.6.1.90-96.1986 ◽

1986 ◽

Vol 6 (1) ◽

pp. 90-96

Author(s):

T McClanahan ◽

K McEntee

Keyword(s):

Saccharomyces Cerevisiae ◽

Dna Damage ◽

Heat Shock ◽

Shock Treatment ◽

Northern Hybridization ◽

Heat Shock Treatment ◽

Base Pairs ◽

S1 Nuclease ◽

Hsp70 Family ◽

Transcriptional Start Sites

Two Saccharomyces cerevisiae genes isolated in a differential hybridization screening for DNA damage regulation (DDR genes) were also transcriptionally regulated by heat shock treatment. A 0.45-kilobase transcript homologous to the DDRA2 gene and a 1.25-kilobase transcript homologous to the DDR48 gene accumulated after exposure of cells to 4-nitroquinoline-1-oxide (NQO; 1 to 1.5 microgram/ml) or brief heat shock (20 min at 37 degrees C). The DDRA2 transcript, which was undetectable in untreated cells, was induced to high levels by these treatments, and the DDR48 transcript increased more than 10-fold as demonstrated by Northern hybridization analysis. Two findings argue that dual regulation of stress-responsive genes is not common in S. cerevisiae. First, two members of the heat shock-inducible hsp70 family of S. cerevisiae, YG100 and YG102, were not induced by exposure to NQO. Second, at least one other DNA-damage-inducible gene, DIN1, was not regulated by heat shock treatment. We examined the structure of the induced RNA homologous to DDRA2 after heat shock and NQO treatments by S1 nuclease protection experiments. Our results demonstrated that the DDRA2 transcript initiates equally frequently at two sites separated by 5 base pairs. Both transcriptional start sites were utilized when cells were exposed to either NQO or heat shock treatment. These results indicate that DDRA2 and DDR48 are members of a unique dually regulated stress-responsive family of genes in S. cerevisiae.

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Enhancement of glycerol production by brewing yeast (Saccharomyces cerevisiae) with heat shock treatment

Journal of Fermentation and Bioengineering ◽

10.1016/0922-338x(96)85048-3 ◽

1996 ◽

Vol 82 (2) ◽

pp. 187-190 ◽

Cited By ~ 29

Author(s):

Toshiro Omori ◽

Kiyoshi Ogawa ◽

Yasufumi Umemoto ◽

Kenji Yuki ◽

Yasuhiro Kajihara ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Heat Shock ◽

Shock Treatment ◽

Heat Shock Treatment ◽

Glycerol Production ◽

Yeast Saccharomyces Cerevisiae ◽

Brewing Yeast

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A novel method for screening high glycerol- and ester-producing brewing yeasts (Saccharomyces cerevisiae) by heat shock treatment

Journal of Fermentation and Bioengineering ◽

10.1016/s0922-338x(97)87329-1 ◽

1997 ◽

Vol 83 (1) ◽

pp. 64-69 ◽

Cited By ~ 10

Author(s):

Toshiro Omori ◽

Yasufumi Umemoto ◽

Kiyoshi Ogawa ◽

Yasuhiro Kajiwara ◽

Masahiko Shimoda ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Heat Shock ◽

Shock Treatment ◽

Heat Shock Treatment ◽

Novel Method ◽

Brewing Yeasts

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Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae.

Molecular and Cellular Biology ◽

10.1128/mcb.11.2.1062 ◽

1991 ◽

Vol 11 (2) ◽

pp. 1062-1068 ◽

Cited By ~ 77

Author(s):

H J Yost ◽

S Lindquist

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Synthesis ◽

Heat Shock ◽

Heat Shock Proteins ◽

Heat Shock Response ◽

Rna Splicing ◽

Yeast Cells ◽

Yeast Saccharomyces Cerevisiae ◽

Shock Response ◽

Shock Proteins

In the yeast Saccharomyces cerevisiae, the splicing of mRNA precursors is disrupted by a severe heat shock. Mild heat treatments prior to severe heat shock protect splicing from disruption, as was previously reported for Drosophila melanogaster. In contrast to D. melanogaster, protein synthesis during the pretreatment is not required to protect splicing in yeast cells. However, protein synthesis is required for the rapid recovery of splicing once it has been disrupted by a sudden severe heat shock. Mutations in two classes of yeast hsp genes affect the pattern of RNA splicing during the heat shock response. First, certain hsp70 mutants, which overproduce other heat shock proteins at normal temperatures, show constitutive protection of splicing at high temperatures and do not require pretreatment. Second, in hsp104 mutants, the recovery of RNA splicing after a severe heat shock is delayed compared with wild-type cells. These results indicate a greater degree of specialization in the protective functions of hsps than has previously been suspected. Some of the proteins (e.g., members of the hsp70 and hsp82 gene families) help to maintain normal cellular processes at higher temperatures. The particular function of hsp104, at least in splicing, is to facilitate recovery of the process once it has been disrupted.

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Heat-induced triploids in Brycon amazonicus: a strategic fish species for aquaculture and conservation

Zygote ◽

10.1017/s0967199421000125 ◽

2021 ◽

pp. 1-5

Author(s):

Nivaldo Ferreira do Nascimento ◽

Rafaela Manchin Bertolini ◽

Lucia Soares Lopez ◽

Laura Satiko Okada Nakaghi ◽

Paulo Sérgio Monzani ◽

...

Keyword(s):

Flow Cytometry ◽

Heat Shock ◽

Early Development ◽

Fish Species ◽

Survival Rates ◽

Shock Treatment ◽

Hatching Rate ◽

Heat Shock Treatment ◽

Control Survival ◽

Ploidy Status

Summary Triploidization plays an important role in aquaculture and surrogate technologies. In this study, we induced triploidy in the matrinxã fish (Brycon amazonicus) using a heat-shock technique. Embryos at 2 min post fertilization (mpf) were heat shocked at 38°C, 40°C, or 42°C for 2 min. Untreated, intact embryos were used as a control. Survival rates during early development were monitored and ploidy status was confirmed using flow cytometry and nuclear diameter analysis of erythrocytes. The hatching rate reduced with heat-shock treatment, and heat-shock treatments at 42°C resulted in no hatching events. Optimal results were obtained at 40°C with 95% of larvae exhibiting triploidy. Therefore, we report that heat-shock treatments of embryos (2 mpf) at 40°C for 2 min is an effective way to induce triploid individuals in B. amazonicus.

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Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression.

The Journal of Cell Biology ◽

10.1083/jcb.106.4.1105 ◽

1988 ◽

Vol 106 (4) ◽

pp. 1105-1116 ◽

Cited By ~ 264

Author(s):

L A Mizzen ◽

W J Welch

Keyword(s):

Protein Synthesis ◽

Heat Shock ◽

Stress Proteins ◽

Stress Protein ◽

Shock Treatment ◽

Heat Shock Treatment ◽

Normal Medium ◽

Growth Environment ◽

Mammalian Cell Lines ◽

C 30

Exposure of mammalian cells to a nonlethal heat-shock treatment, followed by a recovery period at 37 degrees C, results in increased cell survival after a subsequent and otherwise lethal heat-shock treatment. Here we characterize this phenomenon, termed acquired thermotolerance, at the level of translation. In a number of different mammalian cell lines given a severe 45 degrees C/30-min shock and then returned to 37 degrees C, protein synthesis was completely inhibited for as long as 5 h. Upon resumption of translational activity, there was a marked induction of heat-shock (or stress) protein synthesis, which continued for several hours. In contrast, cells first made thermotolerant (by a pretreatment consisting of a 43 degrees C/1.5-h shock and further recovery at 37 degrees C) and then presented with the 45 degrees C/30-min shock exhibited considerably less translational inhibition and an overall reduction in the amount of subsequent stress protein synthesis. The acquisition and duration of such "translational tolerance" was correlated with the expression, accumulation, and relative half-lives of the major stress proteins of 72 and 73 kD. Other agents that induce the synthesis of the stress proteins, such as sodium arsenite, similarly resulted in the acquisition of translational tolerance. The probable role of the stress proteins in the acquisition of translational tolerance was further indicated by the inability of the amino acid analogue, L-azetidine 2-carboxylic acid, an inducer of nonfunctional stress proteins, to render cells translationally tolerant. If, however, analogue-treated cells were allowed to recover in normal medium, and hence produce functional stress proteins, full translational tolerance was observed. Finally, we present data indicating that the 72- and 73-kD stress proteins, in contrast to the other major stress proteins (of 110, 90, and 28 kD), are subject to strict regulation in the stressed cell. Quantitation of 72- and 73-kD synthesis after heat-shock treatment under a number of conditions revealed that "titration" of 72/73-kD synthesis in response to stress may represent a mechanism by which the cell monitors its local growth environment.

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DNA sequence analysis of spontaneous mutations in the SUP4-o gene of Saccharomyces cerevisiae

Molecular and Cellular Biology ◽

10.1128/mcb.8.2.978-981.1988 ◽

1988 ◽

Vol 8 (2) ◽

pp. 978-981

Author(s):

C N Giroux ◽

J R Mis ◽

M K Pierce ◽

S E Kohalmi ◽

B A Kunz

Keyword(s):

Saccharomyces Cerevisiae ◽

Sequence Analysis ◽

Transposable Elements ◽

Dna Sequencing ◽

Dna Sequence ◽

Base Pair ◽

Dna Sequence Analysis ◽

Spontaneous Mutations ◽

Yeast Saccharomyces Cerevisiae ◽

Spontaneous Mutagenesis

A collection of 196 spontaneous mutations in the SUP4-o gene of the yeast Saccharomyces cerevisiae was analyzed by DNA sequencing. The classes of mutation identified included all possible types of base-pair substitution, deletions of various lengths, complex alterations involving multiple changes, and insertions of transposable elements. Our findings demonstrate that at least several different mechanisms are responsible for spontaneous mutagenesis in S. cerevisiae.

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