Characterization of an alternative oxidase activity ofHistoplasma capsulatum

Yeast ◽  
2003 ◽  
Vol 20 (5) ◽  
pp. 381-388 ◽  
Author(s):  
Clayton H. Johnson ◽  
Jonathan T. Prigge ◽  
Aaron D. Warren ◽  
Joan E. McEwen
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase

scholarly journals Stimulation of the alternative oxidase of Neurospora crassa by Nucleoside phosphates

1980 ◽  
Vol 188 (1) ◽  
pp. 141-144 ◽  
Author(s):  
J Vanderleyden ◽  
C Peeters ◽  
H Verachtert ◽  
H Bertrand
Keyword(s):  
Neurospora Crassa ◽  
Oxidase Activity ◽  
Alternative Oxidase ◽  
Purine Nucleoside ◽  
Submitochondrial Particles ◽  
Fold Stimulation ◽  
Succinate Oxidase ◽  
Stimulation Of

The alternative-oxidase-mediated succinate oxidase activity of Neurospora crassa decreases drastically when mitochondria are fractionated into submitochondrial particles or treated with deoxycholate. The activity, however, can be completely restored in the presence of nucleoside 5′-monophosphates. The purine nucleoside 5′-monophosphates are more effective than the pyrimidine homologues. 5′-GMP gives a 10-fold stimulation of the alternative-oxidase-mediated succinate oxidase activity in submitochondrial particles. A comparison is made with the results obtained earlier with Moniliella tomentosa [Hanssens & Verachtert (1976) J. Bacteriol. 125, 825–835; Vanderleyden, Van Den Eynde & Verachtert (1980) Biochem. J. 186, 309–316].

scholarly journals Regulation of Alternative Oxidase Activity by Pyruvate in Soybean Mitochondria

1994 ◽  
Vol 106 (4) ◽  
pp. 1421-1427 ◽  
Author(s):  
D. A. Day ◽  
A. H. Millar ◽  
J. T. Wiskich ◽  
J. Whelan
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase

scholarly journals Immunological identification of the alternative oxidase of Neurospora crassa mitochondria.

1989 ◽  
Vol 9 (3) ◽  
pp. 1362-1364 ◽  
Author(s):  
A M Lambowitz ◽  
J R Sabourin ◽  
H Bertrand ◽  
R Nickels ◽  
L McIntosh
Keyword(s):  
Neurospora Crassa ◽  
Oxidase Activity ◽  
Hydroxamic Acid ◽  
Alternative Oxidase ◽  
Fungal Species ◽  
The Other ◽  
Wild Type ◽  
Higher Plant ◽  
Sauromatum Guttatum ◽  
Immunological Identification

Neurospora crassa mitochondria use a branched electron transport system in which one branch is a conventional cytochrome system and the other is an alternative cyanide-resistant, hydroxamic acid-sensitive oxidase that is induced when the cytochrome system is impaired. We used a monoclonal antibody to the alternative oxidase of the higher plant Sauromatum guttatum to identify a similar set of related polypeptides (Mr, 36,500 and 37,000) that was associated with the alternative oxidase activity of N. crassa mitochondria. These polypeptides were not present constitutively in the mitochondria of a wild-type N. crassa strain, but were produced in high amounts under conditions that induced alternative oxidase activity. Under the same conditions, mutants in the aod-1 gene, with one exception, produced apparently inactive alternative oxidase polypeptides, whereas mutants in the aod-2 gene failed to produce these polypeptides. The latter findings support the hypothesis that aod-1 is a structural gene for the alternative oxidase and that the aod-2 gene encodes a component that is required for induction of alternative oxidase activity. Finally, our results indicate that the alternative oxidase is highly conserved, even between plant and fungal species.

scholarly journals Characterization of the alternative oxidase protein in the yeast Hansenula anomala

FEBS Letters ◽  
1993 ◽  
Vol 318 (3) ◽  
pp. 310-312 ◽  
Author(s):  
Shigeru Sakajo ◽  
Nobuko Minagawa ◽  
Akio Yoshimoto
Keyword(s):  
Alternative Oxidase ◽  
Hansenula Anomala
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