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Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae

The biological function of the trehalose-degrading yeast enzyme neutral trehalase consists of the control of the concentration of trehalose, which is assumed to play a role in thermotolerance, in germination of spores, and in other life functions of yeast. Resequencing of the neutral trehalase gene...

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Published in:The Journal of biological chemistry 1995-04, Vol.270 (17), p.10193-10198
Main Authors: Nwaka, S. (Universitat Freiburg, Freiburg, Germany.), Kopp, M, Holzer, H
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Language:English
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creator Nwaka, S. (Universitat Freiburg, Freiburg, Germany.)
Kopp, M
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description The biological function of the trehalose-degrading yeast enzyme neutral trehalase consists of the control of the concentration of trehalose, which is assumed to play a role in thermotolerance, in germination of spores, and in other life functions of yeast. Resequencing of the neutral trehalase gene NTH1 on chromosome IV resulted in the observation of two possible start codons (Kopp, M., Nwaka, S., and Holzer, H. (1994) Gene (Amst.) 150, 403-404). We show here that only the most upstream start codon which initiates translation of the longest possible ORF is used for expression of NTH1 in vivo . A gene with 77% identity with NTH1 , YBR0106 , which was discovered during sequencing of chromosome II (Wolfe, K. H., and Lohan, A. J. E. (1994) Yeast 10, S41-S46), is shown here to be expressed into mRNA. Experiments with a mutant disrupted in the YBR0106 ORF showed, in contrast to a NTH1 deletion mutant, no changes in trehalase activity and in trehalose concentration. However, similar to the NTH1 gene a requirement of the intact YBR0106 gene for thermotolerance is demonstrated in experiments with the respective mutants. This indicates that the products of the likely duplicated YBR0106 gene and the NTH1 gene serve a heat shock protein function. In case of the YBR0106 gene, this is the only phenotypic feature found at present.
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(Universitat Freiburg, Freiburg, Germany.) ; Kopp, M ; Holzer, H</creator><creatorcontrib>Nwaka, S. (Universitat Freiburg, Freiburg, Germany.) ; Kopp, M ; Holzer, H</creatorcontrib><description>The biological function of the trehalose-degrading yeast enzyme neutral trehalase consists of the control of the concentration of trehalose, which is assumed to play a role in thermotolerance, in germination of spores, and in other life functions of yeast. Resequencing of the neutral trehalase gene NTH1 on chromosome IV resulted in the observation of two possible start codons (Kopp, M., Nwaka, S., and Holzer, H. (1994) Gene (Amst.) 150, 403-404). We show here that only the most upstream start codon which initiates translation of the longest possible ORF is used for expression of NTH1 in vivo . A gene with 77% identity with NTH1 , YBR0106 , which was discovered during sequencing of chromosome II (Wolfe, K. H., and Lohan, A. J. E. 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(Universitat Freiburg, Freiburg, Germany.)</creatorcontrib><creatorcontrib>Kopp, M</creatorcontrib><creatorcontrib>Holzer, H</creatorcontrib><title>Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The biological function of the trehalose-degrading yeast enzyme neutral trehalase consists of the control of the concentration of trehalose, which is assumed to play a role in thermotolerance, in germination of spores, and in other life functions of yeast. Resequencing of the neutral trehalase gene NTH1 on chromosome IV resulted in the observation of two possible start codons (Kopp, M., Nwaka, S., and Holzer, H. (1994) Gene (Amst.) 150, 403-404). We show here that only the most upstream start codon which initiates translation of the longest possible ORF is used for expression of NTH1 in vivo . 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We show here that only the most upstream start codon which initiates translation of the longest possible ORF is used for expression of NTH1 in vivo . A gene with 77% identity with NTH1 , YBR0106 , which was discovered during sequencing of chromosome II (Wolfe, K. H., and Lohan, A. J. E. (1994) Yeast 10, S41-S46), is shown here to be expressed into mRNA. Experiments with a mutant disrupted in the YBR0106 ORF showed, in contrast to a NTH1 deletion mutant, no changes in trehalase activity and in trehalose concentration. However, similar to the NTH1 gene a requirement of the intact YBR0106 gene for thermotolerance is demonstrated in experiments with the respective mutants. This indicates that the products of the likely duplicated YBR0106 gene and the NTH1 gene serve a heat shock protein function. 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identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1995-04, Vol.270 (17), p.10193-10198
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source ScienceDirect Journals
subjects ACID TREHALASE
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Adaptation, Physiological
Base Sequence
BIOCHEMISTRY
BIOCHIMIE
BIOQUIMICA
CALOR
CHALEUR
CHOC
Cloning, Molecular
CYTOCHEMISTRY
DNA Primers
ENZYMIC ACTIVITY
ESTRES TERMICO
EXPRESION GENICA
EXPRESSION DES GENES
GENE
GENE EXPRESSION
GENES
HEAT
HEAT SHOCK
HEAT TOLERANCE
Hot Temperature
Molecular Sequence Data
MUTANT
MUTANTES
MUTANTS
Mutation
NEUTRAL TREHALASE
RESISTANCE A LA TEMPERATURE
RESISTENCIA A LA TEMPERATURA
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - physiology
SHOCK
STRESS THERMIQUE
STRUCTURAL GENES
TEMPERATURE RESISTANCE
THERMAL STRESS
TREHALASA
TREHALASE
Trehalase - genetics
TREHALOSA
TREHALOSE
title Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae
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