Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens

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Standard

Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens. / van den Hazel, H B; Kielland-Brandt, Morten; Winther, Jakob R.

I: European Journal of Biochemistry, Bind 207, Nr. 1, 1992, s. 277-83.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

van den Hazel, HB, Kielland-Brandt, M & Winther, JR 1992, 'Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens', European Journal of Biochemistry, bind 207, nr. 1, s. 277-83.

APA

van den Hazel, H. B., Kielland-Brandt, M., & Winther, J. R. (1992). Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens. European Journal of Biochemistry, 207(1), 277-83.

Vancouver

van den Hazel HB, Kielland-Brandt M, Winther JR. Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens. European Journal of Biochemistry. 1992;207(1):277-83.

Author

van den Hazel, H B ; Kielland-Brandt, Morten ; Winther, Jakob R. / Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens. I: European Journal of Biochemistry. 1992 ; Bind 207, Nr. 1. s. 277-83.

Bibtex

@article{575af08d3ce94709aa037d00937d71a4,
title = "Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens",
abstract = "The Saccharomyces cerevisiae PEP4 gene encodes proteinase A, an aspartyl protease. pep4 mutants are defective in the activation of many vacuolar hydrolases, including proteinase B. We have expressed a pep4 mutation which directs the accumulation of pro-proteinase A with a defective active site. Co-expression with PEP4 leads to normal processing, i.e. the mutant zymogen is functional as a substrate for the maturation reaction in trans. We conclude that wild-type pro-proteinase A has the ability to mediate its own activation. Elimination of the co-expressed PEP4 gene did not effectively stop the processing of the mutant zymogen, owing to a strong, proteinase-B-dependent, phenotypic lag. In a proteinase-B-negative strain, processing of pro-proteinase A led to an active form of a higher molecular mass than the normal mature form.",
keywords = "Alleles, Amino Acid Sequence, Aspartic Acid Endopeptidases, Base Sequence, Binding Sites, Codon, Enzyme Activation, Enzyme Precursors, Genes, Fungal, Molecular Sequence Data, Mutagenesis, Site-Directed, Phenotype, Plasmids, Polymerase Chain Reaction, Protein Processing, Post-Translational, Restriction Mapping, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles",
author = "{van den Hazel}, {H B} and Morten Kielland-Brandt and Winther, {Jakob R.}",
year = "1992",
language = "English",
volume = "207",
pages = "277--83",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Springer Verlag",
number = "1",

}

RIS

TY - JOUR

T1 - Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens

AU - van den Hazel, H B

AU - Kielland-Brandt, Morten

AU - Winther, Jakob R.

PY - 1992

Y1 - 1992

N2 - The Saccharomyces cerevisiae PEP4 gene encodes proteinase A, an aspartyl protease. pep4 mutants are defective in the activation of many vacuolar hydrolases, including proteinase B. We have expressed a pep4 mutation which directs the accumulation of pro-proteinase A with a defective active site. Co-expression with PEP4 leads to normal processing, i.e. the mutant zymogen is functional as a substrate for the maturation reaction in trans. We conclude that wild-type pro-proteinase A has the ability to mediate its own activation. Elimination of the co-expressed PEP4 gene did not effectively stop the processing of the mutant zymogen, owing to a strong, proteinase-B-dependent, phenotypic lag. In a proteinase-B-negative strain, processing of pro-proteinase A led to an active form of a higher molecular mass than the normal mature form.

AB - The Saccharomyces cerevisiae PEP4 gene encodes proteinase A, an aspartyl protease. pep4 mutants are defective in the activation of many vacuolar hydrolases, including proteinase B. We have expressed a pep4 mutation which directs the accumulation of pro-proteinase A with a defective active site. Co-expression with PEP4 leads to normal processing, i.e. the mutant zymogen is functional as a substrate for the maturation reaction in trans. We conclude that wild-type pro-proteinase A has the ability to mediate its own activation. Elimination of the co-expressed PEP4 gene did not effectively stop the processing of the mutant zymogen, owing to a strong, proteinase-B-dependent, phenotypic lag. In a proteinase-B-negative strain, processing of pro-proteinase A led to an active form of a higher molecular mass than the normal mature form.

KW - Alleles

KW - Amino Acid Sequence

KW - Aspartic Acid Endopeptidases

KW - Base Sequence

KW - Binding Sites

KW - Codon

KW - Enzyme Activation

KW - Enzyme Precursors

KW - Genes, Fungal

KW - Molecular Sequence Data

KW - Mutagenesis, Site-Directed

KW - Phenotype

KW - Plasmids

KW - Polymerase Chain Reaction

KW - Protein Processing, Post-Translational

KW - Restriction Mapping

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Vacuoles

M3 - Journal article

C2 - 1628653

VL - 207

SP - 277

EP - 283

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 1

ER -

ID: 43974534