The membrane location of the B890-complex from Rhodospirillum rubrum and the effect of carotenoid on the conformation of its two apoproteins exposed at the cytoplasmic surface

36Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.
Get full text

Abstract

The membrane location of the two B890-apoproteins from Rhodospirillum rubrum has been investigated by comparing the effects of mild proteolysis with proteinase K, and immunoprecipitation, with antibodies prepared against the B890-complex and its individual apoproteins, upon membrane vesicles. By using chromatophores (inside-out vesicles) and spheroplasts (right-side vesicles) both membrane surfaces have been interrogated. The N-terminal regions of both aproproteins are located at the cytoplasmic membrane surface, while the C-termini are most probably located at the periplasmic surface. The conformation of the N-terminal regions of the apoproteins is changed by the presence of carotenoid. In the carotenoid-containing strain S1, for example, the α-apoprotein is insensitive to digestion by proteinase K, while in the absence of the carotenoid in the mutant G9+six amino acids are removed from the N-terminus of the α-aproprotein by proteinase K treatment. © 1986.

Cite

CITATION STYLE

APA

Brunisholz, R. A., Zuber, H., Valentine, J., Lindsay, J. G., Woolley, K. J., & Cogdell, R. J. (1986). The membrane location of the B890-complex from Rhodospirillum rubrum and the effect of carotenoid on the conformation of its two apoproteins exposed at the cytoplasmic surface. BBA - Bioenergetics, 849(3), 295–303. https://doi.org/10.1016/0005-2728(86)90141-6

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free