Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P20020 (
adenosine triphosphatase
)
3,299
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Polyadenylated mRNA was isolated from aged slices of sweet potato root tissue and translated in a wheat germ cell-free system. The synthesis of
apoprotein
of the flavoprotein subunit of succinate dehydrogenase and two of the subunits of mitochondrial
adenosine triphosphatase
were detected by indirect immunoprecipitation. The molecular weights of the immunologically identified products were 3,000 and 8,000-9,000 daltons larger than the mature flavoprotein subunit of succinate dehydrogenase and the mature subunits of
adenosine triphosphatase
, respectively.
...
PMID:Cell-free synthesis of succinate dehydrogenase and mitochondrial adenosine triphosphatase of sweet potato. 613 26
The effects of the mitochondrial protein synthesis inhibitor chloramphenicol and the mitochondrial F0
adenosine triphosphatase
inhibitor oligomycin on the synthesis of nucleus-encoded cytochrome c protein were studied. Both inhibitors stimulated cytochrome c protein synthesis in the derepressed state (growth in media containing 2% raffinose) but had no effect on the synthesis of the cytochrome c protein in the repressed state (growth in media containing 5% glucose). Oligomycin uncoupled the synthesis of the
apoprotein
from its processing into the hemoprotein. Neither antibiotic had a significant effect on the rate of glucose repression of cytochrome protein synthesis. The kinetics of cytochrome c derepression and the effects of these two antibiotics on these kinetics were also studied. Cells were derepressed by transfer from glucose- to faffinose-containing media, and the rate of cytochrome c synthesis increased from the repressed to the derepressed level during the second hour of derepression. Chloramphenicol delayed this derepression, but after 5 h the rate of cytochrome c protein synthesis increased to twice the rate of synthesis in uninhibited cells. On the other hand, oligomycin inhibited derepression of cytochrome c. These results are discussed with respect to the effects of mitochondrial function in the derepressed and repressed states and during the processes of repression and derepression of cytochrome c.
...
PMID:Effect of mitochondrial functions on synthesis of yeast cytochrome c. 624 23
Mitochondrial
adenosine triphosphatase
isolated from a double mutant of Saccharomyces cerevisiae lacking cytochrome b
apoprotein
and subunit II of cytochrome oxidase does not contain the mitochondrial translation product (approximate molecular weight, 32,000) previously suggested to be a subunit of the enzyme complex.
...
PMID:The largest mitochondrial translation product copurifying with the mitochondrial adenosine triphosphatase of Saccharomyces cerevisiae is not a subunit of the enzyme complex. 626 Jul 57