Publication

Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase

Dijk, R. V., Lahchev, K. L., Kram, A. M., Klei, I. J. V. D. & Veenhuis, M., 2002, In : Fems Yeast Research. 1, 4, 7 p.

Research output: Contribution to journalArticleAcademic

APA

Dijk, R. V., Lahchev, K. L., Kram, A. M., Klei, I. J. V. D., & Veenhuis, M. (2002). Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase. Fems Yeast Research, 1(4). https://doi.org/10.1111/j.1567-1364.2002.tb00043.x

Author

Dijk, Ralf van ; Lahchev, Kancho L. ; Kram, Anita M. ; Klei, Ida J. van der ; Veenhuis, Marten. / Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase. In: Fems Yeast Research. 2002 ; Vol. 1, No. 4.

Harvard

Dijk, RV, Lahchev, KL, Kram, AM, Klei, IJVD & Veenhuis, M 2002, 'Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase', Fems Yeast Research, vol. 1, no. 4. https://doi.org/10.1111/j.1567-1364.2002.tb00043.x

Standard

Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase. / Dijk, Ralf van; Lahchev, Kancho L.; Kram, Anita M.; Klei, Ida J. van der; Veenhuis, Marten.

In: Fems Yeast Research, Vol. 1, No. 4, 2002.

Research output: Contribution to journalArticleAcademic

Vancouver

Dijk RV, Lahchev KL, Kram AM, Klei IJVD, Veenhuis M. Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase. Fems Yeast Research. 2002;1(4). https://doi.org/10.1111/j.1567-1364.2002.tb00043.x


BibTeX

@article{58a7235591c54cd097a34d3ec8de14c2,
title = "Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase",
abstract = "Alcohol oxidase (AO) is a peroxisomal enzyme that catalyses the first step in methanol metabolism in yeast. Monomeric, inactive AO protein is synthesised in the cytosol and subsequently imported into peroxisomes, where the enzymatically active, homo-octameric form is found. The mechanisms involved in AO octamer assembly are largely unclear. Here we describe the isolation of Hansenula polymorpha mutants specifically affected in AO assembly. These mutants are unable to grow on methanol and display reduced AO activities. Based on their phenotypes, three major classes of mutants were isolated. Three additional mutants were isolated that each displayed a unique phenotype. Complementation analysis revealed that the isolated AO assembly mutants belonged to 10 complementation groups.",
keywords = "Hansenula polymorpha, Peroxisome, Protein assembly, Alcohol oxidase",
author = "Dijk, {Ralf van} and Lahchev, {Kancho L.} and Kram, {Anita M.} and Klei, {Ida J. van der} and Marten Veenhuis",
note = "Relation: https://www.rug.nl/gbb/ date_submitted:2007 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute",
year = "2002",
doi = "10.1111/j.1567-1364.2002.tb00043.x",
language = "English",
volume = "1",
journal = "Fems Yeast Research",
issn = "1567-1356",
number = "4",

}

RIS

TY - JOUR

T1 - Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase

AU - Dijk, Ralf van

AU - Lahchev, Kancho L.

AU - Kram, Anita M.

AU - Klei, Ida J. van der

AU - Veenhuis, Marten

N1 - Relation: https://www.rug.nl/gbb/ date_submitted:2007 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute

PY - 2002

Y1 - 2002

N2 - Alcohol oxidase (AO) is a peroxisomal enzyme that catalyses the first step in methanol metabolism in yeast. Monomeric, inactive AO protein is synthesised in the cytosol and subsequently imported into peroxisomes, where the enzymatically active, homo-octameric form is found. The mechanisms involved in AO octamer assembly are largely unclear. Here we describe the isolation of Hansenula polymorpha mutants specifically affected in AO assembly. These mutants are unable to grow on methanol and display reduced AO activities. Based on their phenotypes, three major classes of mutants were isolated. Three additional mutants were isolated that each displayed a unique phenotype. Complementation analysis revealed that the isolated AO assembly mutants belonged to 10 complementation groups.

AB - Alcohol oxidase (AO) is a peroxisomal enzyme that catalyses the first step in methanol metabolism in yeast. Monomeric, inactive AO protein is synthesised in the cytosol and subsequently imported into peroxisomes, where the enzymatically active, homo-octameric form is found. The mechanisms involved in AO octamer assembly are largely unclear. Here we describe the isolation of Hansenula polymorpha mutants specifically affected in AO assembly. These mutants are unable to grow on methanol and display reduced AO activities. Based on their phenotypes, three major classes of mutants were isolated. Three additional mutants were isolated that each displayed a unique phenotype. Complementation analysis revealed that the isolated AO assembly mutants belonged to 10 complementation groups.

KW - Hansenula polymorpha

KW - Peroxisome

KW - Protein assembly

KW - Alcohol oxidase

U2 - 10.1111/j.1567-1364.2002.tb00043.x

DO - 10.1111/j.1567-1364.2002.tb00043.x

M3 - Article

VL - 1

JO - Fems Yeast Research

JF - Fems Yeast Research

SN - 1567-1356

IS - 4

ER -

ID: 14671815