The light intensity under which cells are grown controls the type of peripheral light-harvesting complexes that are assembled in a purple photosynthetic bacterium

Author:

Brotosudarmo Tatas H. P.1,Collins Aaron M.2,Gall Andrew3,Roszak Aleksander W.4,Gardiner Alastair T.1,Blankenship Robert E.2,Cogdell Richard J.1

Affiliation:

1. Institute of Molecular Cell and System Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow Biomedical Research Building, 120 University Place, Glasgow G12 8TA, U.K.

2. Departments of Biology and Chemistry, Washington University in St. Louis, Campus Box 1137, 1 Brookings Drive, St. Louis, MO 63130, U.S.A.

3. CEA-Saclay, Institute de Biologie et Technologies de Saclay et CNRS/URA2096, 91191 Gif-sur-Yvette, France

4. School of Chemistry, WestCHEM, University of Glasgow, Glasgow Biomedical Research Building, 120 University Place, Glasgow G12 8TA, U.K.

Abstract

The differing composition of LH2 (peripheral light-harvesting) complexes present in Rhodopseudomonas palustris 2.1.6 have been investigated when cells are grown under progressively decreasing light intensity. Detailed analysis of their absorption spectra reveals that there must be more than two types of LH2 complexes present. Purified HL (high-light) and LL (low-light) LH2 complexes have mixed apoprotein compositions. The HL complexes contain PucABa and PucABb apoproteins. The LL complexes contain PucABa, PucABd and PucBb-only apoproteins. This mixed apoprotein composition can explain their resonance Raman spectra. Crystallographic studies and molecular sieve chromatography suggest that both the HL and the LL complexes are nonameric. Furthermore, the electron-density maps do not support the existence of an additional Bchl (bacteriochlorophyll) molecule; rather the density is attributed to the N-termini of the α-polypeptide.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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