scholarly journals Isolation and characterization of cold sensitive pex6 mutant of the methylotrophic yeast Hansenula polymorpha

2002 ◽  
Vol 18 (2) ◽  
pp. 131-134 ◽  
Author(s):  
V. Y. Nazarko ◽  
O. D. Pochapinsky ◽  
T. Y. Nazarko ◽  
O. V. Stasyk ◽  
A. A. Sibirny
Keyword(s):  
Hansenula Polymorpha ◽  
Methylotrophic Yeast ◽  
Isolation And Characterization ◽  
Cold Sensitive

scholarly journals Isolation and Characterization of Mutants of the Methylotrophic Yeast,Candida boidiniiS2 That Are Impaired in Growth on Peroxisome-Inducing Carbon Sources

1995 ◽  
Vol 59 (5) ◽  
pp. 869-875 ◽  
Author(s):  
Yasuyoshi Sakai ◽  
Hideaki Matsuo ◽  
Kai-Ze He ◽  
Atsushi Saiganji ◽  
Hiroya Yurimoto ◽  
...  
Keyword(s):  
Carbon Sources ◽  
Methylotrophic Yeast ◽  
Isolation And Characterization

scholarly journals The Hansenula polymorpha PER8 gene encodes a novel peroxisomal integral membrane protein involved in proliferation.

1995 ◽  
Vol 128 (3) ◽  
pp. 307-319 ◽  
Author(s):  
X Tan ◽  
H R Waterham ◽  
M Veenhuis ◽  
J M Cregg
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Hansenula Polymorpha ◽  
Methylotrophic Yeast ◽  
Integral Membrane Protein ◽  
Peroxisome Biogenesis ◽  
Primary Sequence ◽  
Zinc Finger Motifs ◽  
Molecular Machinery

We previously described the isolation of mutants of the methylotrophic yeast Hansenula polymorpha that are defective in peroxisome biogenesis. Here, we describe the characterization of one of these mutants, per8, and the cloning of the PER8 gene. In either methanol or methylamine medium, conditions that normally induce the organelles, per8 cells contain no peroxisome-like structures and peroxisomal enzymes are located in the cytosol. The sequence of PER8 predicts that its product (Per8p) is a novel polypeptide of 34 kD, and antibodies against Per8p recognize a protein of 31 kD. Analysis of the primary sequence of Per8p revealed a 39-amino-acid cysteine-rich segment with similarity to the C3HC4 family of zinc-finger motifs. Overexpression of PER8 results in a markedly enhanced increase in peroxisome numbers. We show that Per8p is an integral membrane protein of the peroxisome and that it is concentrated in the membranes of newly formed organelles. We propose that Per8p is a component of the molecular machinery that controls the proliferation of this organelle.

Cloning and biochemical characterization of hexokinase from the methylotrophic yeast Hansenula polymorpha

2003 ◽  
Vol 44 (5) ◽  
pp. 268-276 ◽  
Author(s):  
Helen Karp ◽  
Aiki J�rviste ◽  
Thomas M. Kriegel ◽  
Tiina Alam�e
Keyword(s):  
Biochemical Characterization ◽  
Hansenula Polymorpha ◽  
Methylotrophic Yeast

scholarly journals Second-site suppressors of a cold-sensitive external scaffolding protein of bacteriophage phi X174.

Genetics ◽  
1993 ◽  
Vol 134 (4) ◽  
pp. 1003-1011 ◽  
Author(s):  
B A Fane ◽  
S Shien ◽  
M Hayashi
Keyword(s):  
Coat Protein ◽  
Protein A ◽  
Dna Binding Protein ◽  
Scaffolding Protein ◽  
Major Coat Protein ◽  
Isolation And Characterization ◽  
Initial Characterization ◽  
Cold Sensitive ◽  
Allele Specificity

Abstract This report describes the isolation and characterization of second-site suppressors of a cold-sensitive (cs) external scaffolding protein, gpD, of bacteriophage phi X174. Seven genetically distinct suppressors were isolated. Six of them are located in gene F which encodes the major coat protein of the virus. The seventh is located in gene J which encodes the DNA-binding protein. A subset of the suppressors are trans-acting. These second-site suppressors do not exhibit allele specificity; they are able to suppress defects associated with a csD protein for which they were not selected. The initial characterization of the second-site suppressors and their locations within the major coat protein suggest that the mechanism of suppression may involve both structural and stoichiometric phenomena.

Pichia pastoris as a host system for transformations

1985 ◽  
Vol 5 (12) ◽  
pp. 3376-3385
Author(s):  
J M Cregg ◽  
K J Barringer ◽  
A Y Hessler ◽  
K R Madden
Keyword(s):  
Pichia Pastoris ◽  
Auxotrophic Mutant ◽  
Methylotrophic Yeast ◽  
Fusion Procedure ◽  
Methylotrophic Yeast Pichia Pastoris ◽  
Isolation And Characterization ◽  
Mutant Host ◽  
Histidinol Dehydrogenase ◽  
His4 Gene

We developed a methylotrophic yeast, Pichia pastoris, as a host for DNA transformations. The system is based on an auxotrophic mutant host of P. pastoris which is defective in histidinol dehydrogenase. As a selectable marker, we isolated and characterized the P. pastoris HIS4 gene. Plasmid vectors which contained either the P. pastoris or the Saccharomyces cerevisiae HIS4 gene transformed the P. pastoris mutant host. DNA transfer was accomplished by a modified version of the spheroplast generation (CaCl2-polyethylene glycol)-fusion procedure developed for S. cerevisiae. In addition, we report the isolation and characterization of P. pastoris DNA fragments with autonomous replication sequence activity. Two fragments, PARS1 and PARS2, when present on plasmids increased transformation frequencies to 10(5)/micrograms and maintained the plasmids as autonomous elements in P. pastoris cells.

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