Functions of Conserved Tryptophan Residues of the Core Light-Harvesting Complex ofRhodobactersphaeroides†

Biochemistry ◽  
1997 ◽  
Vol 36 (10) ◽  
pp. 2772-2778 ◽  
Author(s):  
James N. Sturgis ◽  
John D. Olsen ◽  
Bruno Robert ◽  
C. Neil Hunter

1995 ◽  
Vol 99 (43) ◽  
pp. 16179-16191 ◽  
Author(s):  
Stephen E. Bradforth ◽  
Ralph Jimenez ◽  
Frank van Mourik ◽  
Rienk van Grondelle ◽  
Graham R. Fleming


FEBS Letters ◽  
2002 ◽  
Vol 519 (1-3) ◽  
pp. 164-168 ◽  
Author(s):  
Zheng-Yu Wang ◽  
Masahiro Shimonaga ◽  
Masayuki Kobayashi ◽  
Tsunenori Nozawa


1994 ◽  
Vol 40 (3) ◽  
pp. 231-245 ◽  
Author(s):  
Paul A. Loach ◽  
Pamela S. Parkes-Loach ◽  
Christine M. Davis ◽  
Barbara A. Heller


2015 ◽  
Vol 83 (5) ◽  
pp. 845-852 ◽  
Author(s):  
Eleonora Sendersky ◽  
Noga Kozer ◽  
Mali Levi ◽  
Michael Moizik ◽  
Yuval Garini ◽  
...  


2005 ◽  
Vol 187 (4) ◽  
pp. 1334-1343 ◽  
Author(s):  
Muktak Aklujkar ◽  
Roger C. Prince ◽  
J. Thomas Beatty

ABSTRACT The core of the photosynthetic apparatus of purple photosynthetic bacteria such as Rhodobacter capsulatus consists of a reaction center (RC) intimately associated with light-harvesting complex 1 (LH1) and the PufX polypeptide. The abundance of the RC and LH1 components was previously shown to depend on the product of the puhB gene (formerly known as orf214). We report here that disruption of puhB diminishes RC assembly, with an indirect effect on LH1 assembly, and reduces the amount of PufX. Under semiaerobic growth conditions, the core complex was present at a reduced level in puhB mutants. After transfer of semiaerobically grown cultures to photosynthetic (anaerobic illuminated) conditions, the RC/LH1 complex became only slightly more abundant, and the amount of PufX increased as cells began photosynthetic growth. We discovered that the photosynthetic growth of puhB disruption strains of R. capsulatus starts after a long lag period, which is due to physiological adaptation rather than secondary mutations. Using a hybrid protein expression system, we determined that the three predicted transmembrane segments of PuhB are capable of spanning a cell membrane and that the second transmembrane segment could mediate self-association of PuhB. We discuss the possible function of PuhB as a dimeric RC assembly factor.



Sign in / Sign up

Export Citation Format

Share Document