Location of catalase in crystalline peroxisomes of methanol-grown Hansenula polymorpha
نویسندگان
چکیده
منابع مشابه
Methanol oxidation and assimilation in Hansenula polymorpha
The metabolism of methanol was monitored in whole cells of the methylotrophic yeast Hansenula polymorpha by using [13C]methanol and n.m.r. in vivo. The main products observed under normal conditions were trehalose and glycerol, whereas cells that were starved before exposure to [13C]methanol also accumulated glutamate, glutamine and alanine; formate was also more prominent in spectra from starv...
متن کاملHansenula polymorpha Swi1p and Snf2p are essential for methanol utilisation.
We have cloned the Hansenula polymorpha SWI1 and SNF2 genes by functional complementation of mutants that are defective in methanol utilisation. These genes encode proteins similar to Saccharomyces cerevisiae Swi1p and Snf2p, which are subunits of the SWI/SNF complex. This complex belongs to the family of nucleosome-remodeling complexes that play a role in transcriptional control of gene expres...
متن کاملPexophagy in Hansenula polymorpha.
In the yeast Hansenula polymorpha the development and turnover of peroxisomes is readily achieved by manipulation of the cultivation conditions. The organelles massively develop when the cells are incubated in the presence of methanol as the sole source of carbon and energy. However, they are rapidly and selectively degraded when methanol-grown cells are placed at conditions of repression of me...
متن کاملDamaged peroxisomes are subject to rapid autophagic degradation in the yeast Hansenula polymorpha.
Evidence is accumulating that damaged components of eukaryotic cells are removed by autophagic degradation (e.g., mitophagy). Here we show that peroxisomes that are damaged by the abrupt removal of the membrane protein Pex3 are massively and rapidly degraded even when the cells are placed at peroxisome-inducing conditions and hence need the organelles for growth. Pex3 degradation was induced by...
متن کاملHARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization.
The HARO7 gene of the methylotrophic, thermotolerant yeast Hansenula polymorpha was cloned by functional complementation. HARO7 encodes a monofunctional 280-amino-acid protein with chorismate mutase (EC 5.4. 99.5) activity that catalyzes the conversion of chorismate to prephenate, a key step in the biosynthesis of aromatic amino acids. The HARO7 gene product shows strong similarities to primary...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1992
ISSN: 0378-1097
DOI: 10.1016/0378-1097(92)90481-3