Hansenula polymorpha: Biology and Applications. Edited by G. Gellissen. Wiley-VCH, Weinham, 2002

Yeast ◽  
2003 ◽  
Vol 20 (15) ◽  
pp. 1307-1308 ◽  
Author(s):  
Peter Sudbery
Keyword(s):  
Hansenula Polymorpha

Investigations on the possible role of the endoplasmic reticulum in the development of peroxisomes in the yeast Hansenula polymorpha

1985 ◽  
Vol 51 (5-6) ◽  
pp. 572-572
Author(s):  
M. Veenhuis ◽  
A. C. Douma ◽  
P. G. Bruinenberg ◽  
W. Harder
Keyword(s):  
Endoplasmic Reticulum ◽  
Hansenula Polymorpha

scholarly journals Watermelon glyoxysomal malate dehydrogenase is sorted to peroxisomes of the methylotrophic yeast, Hansenula polymorpha

FEBS Letters ◽  
1993 ◽  
Vol 334 (1) ◽  
pp. 128-132 ◽  
Author(s):  
I.J. van der Klei ◽  
K.N. Faber ◽  
I. Keizer-Gunnink ◽  
C. Gietl ◽  
W. Harder ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Hansenula Polymorpha ◽  
Methylotrophic Yeast

Scarless gene deletion in methylotrophic Hansenula polymorpha by using mazF as counter-selectable marker

2015 ◽  
Vol 468 ◽  
pp. 66-74 ◽  
Author(s):  
Panpan Song ◽  
Sha Liu ◽  
Xuena Guo ◽  
Xuejing Bai ◽  
Xiuping He ◽  
...  
Keyword(s):  
Gene Deletion ◽  
Selectable Marker ◽  
Hansenula Polymorpha

Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

1989 ◽  
Vol 1008 (2) ◽  
pp. 157-167 ◽  
Author(s):  
Paul G Bruinenberg ◽  
Melchior Evers ◽  
Hans R Waterham ◽  
Jeroen Kuipers ◽  
Annika C Arnberg ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Hansenula Polymorpha ◽  
Cloning And Sequencing ◽  
Oxidase Gene

scholarly journals Pyruvate Carboxylase Is an Essential Protein in the Assembly of Yeast Peroxisomal Oligomeric Alcohol Oxidase

2003 ◽  
Vol 14 (2) ◽  
pp. 786-797 ◽  
Author(s):  
Paulina Ozimek ◽  
Ralf van Dijk ◽  
Kantcho Latchev ◽  
Carlos Gancedo ◽  
Dong Yuan Wang ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Tricarboxylic Acid Cycle ◽  
Hansenula Polymorpha ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeast ◽  
Tricarboxylic Acid ◽  
Matrix Proteins ◽  
Growth Media ◽  
Fad Binding

Hansenula polymorpha ass3 mutants are characterized by the accumulation of inactive alcohol oxidase (AO) monomers in the cytosol, whereas other peroxisomal matrix proteins are normally activated and sorted to peroxisomes. These mutants also have a glutamate or aspartate requirement on minimal media. Cloning of the corresponding gene resulted in the isolation of the H. polymorpha PYC gene that encodes pyruvate carboxylase (HpPyc1p). HpPyc1p is a cytosolic, anapleurotic enzyme that replenishes the tricarboxylic acid cycle with oxaloacetate. The absence of this enzyme can be compensated by addition of aspartate or glutamate to the growth media. We show that HpPyc1p protein but not the enzyme activity is essential for import and assembly of AO. Similar results were obtained in the related yeast Pichia pastoris. In vitro studies revealed that HpPyc1p has affinity for FAD and is capable to physically interact with AO protein. These data suggest that in methylotrophic yeast pyruvate carboxylase plays a dual role in that, besides its well-characterized metabolic function as anapleurotic enzyme, the protein fulfils a specific role in the AO sorting and assembly process, possibly by mediating FAD-binding to AO monomers.

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