Journal article

Publication year: 1990

Pages: 7754-7758

Journal: Biochemistry

Volume number: 29

Issue number: 33

ISSN: 0006-2960

DOI Link: https://doi.org/10.1021/bi00485a026

Publisher: American Chemical Society

Abstract: 

The N-terminal domains of the a and /? polypeptides of the B870 antenna complex
of Rhodobacter capsulatus are oppositely charged. In both polypeptides two charged
amino acids are located close to the N-terminus, and two of them are close to the
hydrophobic central domain. To test the hypothesis that charged amino acids in the
N-terminus have a function for insertion and assembly of pigment-binding polypeptides,
charged amino acids were replaced by amino acids of opposite charge. The results
show that an exchange of amino acid positions 3 and 6 in a (Lys -  Glu) or 2 and 5 in /? (Asp —*• Lys, Arg) has little
effect under semiaerobic conditions on the formation of B870 but the additional
exchange of positions 14 and 15 in a (Arg —  Glu, Asp) and/or 13 and 14 in /3 (Asp, Glu —  Arg) inhibits strongly under semiaerobic dark and
anaerobic light conditions the stable incorporation of the polypeptides into the
membrane and the formation of the B870 complex. The mutant U43(pTXAB5) is able to
grow without any antenna.  

Harvard Citation style: Dorge, B., KlugG, Gadon, N., Cohen, S. and Drews, G. (1990) Effects on the formation of antenna complex B870 of Rhodobacter capsulatus by exchange of charged amino acids in the N-terminal domain of the .alpha. and .beta. pigment-binding proteins, Biochemistry, 29(33), pp. 7754-7758. https://doi.org/10.1021/bi00485a026

APA Citation style: Dorge, B., KlugG, Gadon, N., Cohen, S., & Drews, G. (1990). Effects on the formation of antenna complex B870 of Rhodobacter capsulatus by exchange of charged amino acids in the N-terminal domain of the .alpha. and .beta. pigment-binding proteins. Biochemistry. 29(33), 7754-7758. https://doi.org/10.1021/bi00485a026