5830
1975
eng
article
1
2012-05-06
--
--
Identification of two products of mitochondrial protein synthesis associated with mitochondrial adenosine triphosphatase from Neurospora crassa
Soluble mitochondrial ATPase (F1) isolated from Neurospora crassa is resolved by dodecylsulfate- gel electrophoresis into five polypeptide bands with apparent molecular weights of 59000, 55000, 36000, 15000 and 12000. At least nine further polypeptides remain associated with ATPase after disintegration of mitochondria with Triton X-100 as shown by the analysis of an immunoprecipitate obtained with antiserum to F 1 A TPase. Two of the associated polypeptides with apparent molecular weights of 19000 and 11000 are translated on mitochondrial ribosomes, as demonstrated by incorporation in vivo of radioactive leueine in the presence of specific inhibitors of mitochondrial (chloramphenicol) and extramitochondrial ( cycloheximide) protein synthesis. The appearance of mitochondrial translation products in the immunoprecipitated A TPase complex is inhibited by' cycloheximide. The same applies for some of the extramitochondrial translation products in the presence of chloramphenicol. This suggests that both types of polypeptides are necessary for the assembly of the A TPase complex.
urn:nbn:de:bvb:20-opus-62812
6281
In: European Journal of Biochemistry (1975 May) 54(1) 97-106.
Deutsches Urheberrecht
G. Jackl
Walter Sebald
deu
swd
Biochemie
Biowissenschaften; Biologie
open_access
Theodor-Boveri-Institut für Biowissenschaften
Universität Würzburg
https://opus.bibliothek.uni-wuerzburg.de/files/5830/Sebald60.pdf
5834
1972
eng
article
1
2012-05-06
--
--
Inhibition of the assembly of cytochrome oxidase in Neurospora crassa by chloramphenicol
Cytochrome oxidasewas prepared from Neurospora crassa by chromatography on oleyl polymethacrylic acid resin and separated into seven polypeptides by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate. Incorporation oflabelled amino acids into the single polypeptideswas investigated after a pulse labelling in the absence and presence of chloramphenicol, and afterwashing out the inhibitor. Chloramphenicol (4 mg/ml) inhibited amino acid incorporation into all polypeptides 90-95%• while labeHing of the whole membrane protein was inhibited only 30%• Mter washing out the inhibitor and further growth of the cells. the four smaller polypeptides were highly labelled, whereas the other polypeptides showed only a. small increase in radioactivity. It is concluded that the four small-sized polypeptides of cytochrome oxidase are synthesized but not integrated into the functional enzyme under the action of chloramphenicol.
urn:nbn:de:bvb:20-opus-62852
6285
In: European Journal of Biochemistry (1972 Nov 7) 30(3) 413-417.
Deutsches Urheberrecht
Walter Sebald
H. Weiss
G. Jackl
deu
swd
Biochemie
Biowissenschaften; Biologie
open_access
Theodor-Boveri-Institut für Biowissenschaften
Universität Würzburg
https://opus.bibliothek.uni-wuerzburg.de/files/5834/Sebald65.pdf
915
1972
deu
article
1
2013-12-03
--
--
Über die Abhängigkeit des Zusammenbaus der Cytochromoxidase von der Anwesenheit der Produkte der mitochondrialen Proteinsynthese
Dependence of the structure of cytochrome oxidase on the presence of products from mitochondrial protein synthesis
no abstract available
urn:nbn:de:bvb:20-opus-84192
8419
In: Hoppe-Seyler's Zeitschrift für physiologische Chemie (1972) 353, 5, 757.
Deutsches Urheberrecht
Walter Sebald
H. Weiss
G. Jackl
deu
swd
Physiologische Chemie
Biowissenschaften; Biologie
open_access
Theodor-Boveri-Institut für Biowissenschaften
Universität Würzburg
https://opus.bibliothek.uni-wuerzburg.de/files/915/Sebald66.pdf
6898
1974
eng
article
1
2013-12-03
--
--
Identification of two products of mitochondrial protein synthesis associated with oligomycin-sensitive ATPase from Neurospora crassa
no abstract available
urn:nbn:de:bvb:20-opus-82093
8209
In: Hoppe-Seyler's Zeitschrift für physiologische Chemie (1974) 355, 10, 1211-2.
Deutsches Urheberrecht
G. Jackl
Walter Sebald
deu
swd
Physiologische Chemie
Biowissenschaften; Biologie
open_access
Theodor-Boveri-Institut für Biowissenschaften
Universität Würzburg
https://opus.bibliothek.uni-wuerzburg.de/files/6898/Sebald61.pdf