TY - JOUR
T1 - Biosynthesis of chlorosome proteins is not inhibited in acetylene-treated cultures of Chlorobium vibrioforme
AU - Vassilieva, Elena V.
AU - Ormerod, John G.
AU - Bryant, Donald A.
N1 - Funding Information:
This work was supported by grant DE-FG02-94ER20137 from the US Department of Energy to D. A. B. The authors would like to thank Dr R. E. Blankenship, Arizona State University, for providing the antiserum to the FmoA protein and Dr Niels-Ulrik Frigaard for critically reading the manuscript.
PY - 2002
Y1 - 2002
N2 - The composition, abundance and apparent molecular masses of chlorosome polypeptides from Chlorobium tepidum and Chlorobium vibrioforme 8327 were compared. The most abundant, low-molecular-mass chlorosome polypeptides of both strains had similar electrophoretic mobilities and abundances, but several of the larger proteins were different in both apparent mass and abundance. Polyclonal antisera raised against recombinant chlorosome proteins of Cb. tepidum recognized the homologous proteins in Cb. vibrioforme, and a one-to-one correspondence between the chlorosome proteins of the two species was confirmed. As previously shown [Ormerod et al. (1990) J Bacteriol 172: 1352-1360], acetylene strongly suppressed the synthesis of bacteriochlorophyll c in Cb. vibrioforme strain 8327. No correlation was found between the bacteriochlorophyll c content of cells and the cellular content of chlorosome proteins. Nine of ten chlorosome proteins were detected in acetylene-treated cultures, and the chlorosome proteins were generally present in similar amounts in control and acetylene-treated cells. These results suggest that the synthesis of chlorosome proteins and the assembly of the chlorosome envelope is constitutive. It remains possible that the synthesis of bacteriochlorophyll c and its insertion into chlorosomes might be regulated by environmental parameters such as light intensity.
AB - The composition, abundance and apparent molecular masses of chlorosome polypeptides from Chlorobium tepidum and Chlorobium vibrioforme 8327 were compared. The most abundant, low-molecular-mass chlorosome polypeptides of both strains had similar electrophoretic mobilities and abundances, but several of the larger proteins were different in both apparent mass and abundance. Polyclonal antisera raised against recombinant chlorosome proteins of Cb. tepidum recognized the homologous proteins in Cb. vibrioforme, and a one-to-one correspondence between the chlorosome proteins of the two species was confirmed. As previously shown [Ormerod et al. (1990) J Bacteriol 172: 1352-1360], acetylene strongly suppressed the synthesis of bacteriochlorophyll c in Cb. vibrioforme strain 8327. No correlation was found between the bacteriochlorophyll c content of cells and the cellular content of chlorosome proteins. Nine of ten chlorosome proteins were detected in acetylene-treated cultures, and the chlorosome proteins were generally present in similar amounts in control and acetylene-treated cells. These results suggest that the synthesis of chlorosome proteins and the assembly of the chlorosome envelope is constitutive. It remains possible that the synthesis of bacteriochlorophyll c and its insertion into chlorosomes might be regulated by environmental parameters such as light intensity.
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U2 - 10.1023/A:1014903630687
DO - 10.1023/A:1014903630687
M3 - Article
AN - SCOPUS:0036232135
SN - 0166-8595
VL - 71
SP - 69
EP - 81
JO - Photosynthesis research
JF - Photosynthesis research
IS - 1-2
ER -