نتایج جستجو برای: hansenula polymorpha

تعداد نتایج: 1687  

2015
Ann S. Thomas Arjen M. Krikken Ida J. van der Klei Chris P. Williams

Pex11p plays a crucial role in peroxisomal fission. Studies in Saccharomyces cerevisiae and Pichia pastoris indicated that Pex11p is activated by phosphorylation, which results in enhanced peroxisome proliferation. In S. cerevisiae but not in P. pastoris, Pex11p phosphorylation was shown to regulate the protein's trafficking to peroxisomes. However, phosphorylation of PpPex11p was proposed to i...

Journal: :The Biochemical journal 1996
N Brito J Avila M D Perez C Gonzalez J M Siverio

The nitrite reductase-encoding gene (YNI1) from the yeast Hansenula polymorpha was isolated from a lambda EMBL3 H. polymorpha genomic DNA library, using as a probe a 481 bp DNA fragment from the gene of Aspergillus nidulans encoding nitrite reductase (niiA). An open reading frame of 3132 bp, encoding a putative protein of 1044 amino acids with high similarity with nitrite reductases from fungi,...

Journal: :FEMS microbiology letters 2004
Wanida Wongsumpanchai Sarintip Anamnart Kobkul Laoteng Amorn Petsom

Fatty acid elongation defective mutant was isolated from the ethyl methanesulfonate treated Hansenula polymorpha based on the growth ability. Using biochemical and genetic approaches, the mutant was characterized. When compared with the fatty acid phenotype of the parental strain, the differences in profile and content of fatty acids in V1 mutant were found. In this V1 mutant, polyunsaturated f...

Journal: :FEMS yeast research 2003
Oleh V Stasyk Volodymyr Y Nazarko Olexiy D Pochapinsky Taras Y Nazarko Marten Veenhuis Andrei A Sibirny

Two interacting AAA ATPases, Pex1p and Pex6p, are indispensable for peroxisome biogenesis in different organisms. Mutations affecting corresponding genes are the most common cause of the peroxisome biogenesis disorders in humans. By UV mutagenesis of the Hansenula polymorpha pex6 mutant, deficient in peroxisome biogenesis, we isolated a conditional cold-sensitive strain with restored ability to...

2009
Loknath Gidijala Jan A. K. W. Kiel Rutger D. Douma Reza M. Seifar Walter M. van Gulik Roel A. L. Bovenberg Marten Veenhuis Ida J. van der Klei

This study aimed at developing an alternative host for the production of penicillin (PEN). As yet, the industrial production of this beta-lactam antibiotic is confined to the filamentous fungus Penicillium chrysogenum. As such, the yeast Hansenula polymorpha, a recognized producer of pharmaceuticals, represents an attractive alternative. Introduction of the P. chrysogenum gene encoding the non-...

Journal: :Microbial Cell Factories 2006
Franz S Hartner Anton Glieder

Methylotrophic yeasts such as Candida boidinii, Hansenula polymorpha, Pichia methanolica and Pichia pastoris are an emerging group of eukaryotic hosts for recombinant protein production with an ever increasing number of applications during the last 30 years. Their applications are linked to the use of strong methanol-inducible promoters derived from genes of the methanol utilisation pathway. Th...

Journal: :International microbiology : the official journal of the Spanish Society for Microbiology 1998
A Domínguez E Fermiñán M Sánchez F J González F M Pérez-Campo S García A B Herrero A San Vicente J Cabello M Prado F J Iglesias A Choupina F J Burguillo L Fernández-Lago M C López

Yeasts are an attractive group of lower eukaryotic microorganisms, some of which are used in several industrial processes that include brewing, baking and the production of a variety of biochemical compounds. More recently, yeasts have been developed as host organisms for the production of foreign (heterologous) proteins. Saccharomyces cerevisiae has usually been the yeast of choice, but an inc...

Journal: :Journal of cell science 2005
Marleen Otzen Dongyuan Wang Marcel G J Lunenborg Ida J van der Klei

We have cloned and characterized the Hansenula polymorpha PEX20 gene. The HpPEX20 gene encodes a protein of 309 amino acids (HpPex20p) with a calculated molecular mass of approximately 35 kDa. In cells of an HpPEX20 disruption strain, PTS2 proteins were mislocalized to the cytosol, whereas PTS1 matrix protein import proceeded normally. Also, the PTS2 proteins amine oxidase and thiolase were nor...

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