The topology of the proton translocating F\(_0\) component of the ATP synthase from E. coli K12: studies with proteases
Please always quote using this URN: urn:nbn:de:bvb:20-opus-62718
- The accessibility of the three F\(_0\) subunits a, b and c from the Escherichia coli Kll A TP synthase to various proteases was studied in F\(_1\)-depleted inverted membrane vesicles. Subunit b was very sensitive to all applied proteases. Chymotrypsin produced a defined fragment of mol. wt. 1S 000 which remained tightly bound to the membrane. The cleavage site was located at the C-terminal region of subunit b. Larger amounts of proteases were necessary to attack subunit a (mol. wt. 30 000). There was no detectable deavage of subunit c. It isThe accessibility of the three F\(_0\) subunits a, b and c from the Escherichia coli Kll A TP synthase to various proteases was studied in F\(_1\)-depleted inverted membrane vesicles. Subunit b was very sensitive to all applied proteases. Chymotrypsin produced a defined fragment of mol. wt. 1S 000 which remained tightly bound to the membrane. The cleavage site was located at the C-terminal region of subunit b. Larger amounts of proteases were necessary to attack subunit a (mol. wt. 30 000). There was no detectable deavage of subunit c. It is suggested that the major hydrophilic part of subunit b extends from the membrane into the cytoplasm and is in contact with the F\(_1\) sector. The F\(_1\) sector was found to afford some protection against proteolysis oftheb subunit in vitro andin vivo. Protease digestion bad no influence on the electro-impelled H\(^+\) conduction via F\(_0\) bot ATP-dependent H\(^+\) translocation could not be reconstituted upon binding of F\(_1\)• A possible role for subunit b as a linker between catalytic events on the F\(_1\) component and the proton pathway across the membrane is discussed.…
Author: | J. Hoppe, P. Friedl, H. U. Schairer, Walter Sebald, K. von Meyenburg, B. B. Jorgensen |
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URN: | urn:nbn:de:bvb:20-opus-62718 |
Document Type: | Journal article |
Faculties: | Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften |
Language: | English |
Year of Completion: | 1983 |
Source: | In: EMBO Journal (1983) 2(1), 105-10. |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
GND Keyword: | Biochemie |
Tag: | ATPase mutants; protein pathway |
Release Date: | 2012/04/27 |
Licence (German): | Deutsches Urheberrecht |