Nine Mutants of Chlorobium tepidum Each Unable to Synthesize a Different Chlorosome Protein Still Assemble Functional Chlorosomes

Niels Ulrik Frigaard, Hui Li, Kirstin J. Milks, Donald Ashley Bryant

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Chlorosomes of the green sulfur bacterium Chlorobium tepidum comprise mostly bacteriochlorophyll c (BChl c), small amounts of BChl a, carotenoids, and quinones surrounded by a lipid-protein envelope. These structures contain 10 different protein species (CsmA, CsmB, CsmC, CsmD, CsmE, CsmF, CsmH, CsmI, CsmJ, and CsmX) but contain relatively little total protein compared to other photosynthetic antenna complexes. Except for CsmA, which has been suggested to bind BChl a, the functions of the chlorosome proteins are not known. Nine mutants in which a single csm gene was inactivated were created; these mutants included genes encoding all chlorosome proteins except CsmA. All mutants had BChl c contents similar to that of the wild-type strain and had growth rates indistinguishable from or within ∼90% (CsmC- and CsmJ -) of those of the wildtype strain. Chlorosomes isolated from the mutants lacked only the protein whose gene had been inactivated and were generally similar to those from the wild-type strain with respect to size, shape, and BChl c, BChl a, and carotenoid contents. However, chlorosomes from the csmC mutant were about 25% shorter than those from the wild-type strain, and the BChl c absorbance maximum was blue-shifted about 8 nm, indicating that the structure of the BChl c aggregates in these chlorosomes is altered. The results of the present study establish that, except with CsmA, when the known chlorosome proteins are eliminated individually, none of them are essential for the biogenesis, light harvesting, or structural organization of BChl c and BChl a within the chlorosome. These results demonstrate that chlorosomes are remarkably robust structures that can tolerate considerable changes in protein composition.

Original languageEnglish (US)
Pages (from-to)646-653
Number of pages8
JournalJournal of bacteriology
Volume186
Issue number3
DOIs
StatePublished - Feb 1 2004

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Chlorobium
Proteins
Carotenoids
Chlorobi
Photosynthetic Reaction Center Complex Proteins
Quinones
Genes
bacteriochlorophyll c
Lipids
Light

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

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title = "Nine Mutants of Chlorobium tepidum Each Unable to Synthesize a Different Chlorosome Protein Still Assemble Functional Chlorosomes",
abstract = "Chlorosomes of the green sulfur bacterium Chlorobium tepidum comprise mostly bacteriochlorophyll c (BChl c), small amounts of BChl a, carotenoids, and quinones surrounded by a lipid-protein envelope. These structures contain 10 different protein species (CsmA, CsmB, CsmC, CsmD, CsmE, CsmF, CsmH, CsmI, CsmJ, and CsmX) but contain relatively little total protein compared to other photosynthetic antenna complexes. Except for CsmA, which has been suggested to bind BChl a, the functions of the chlorosome proteins are not known. Nine mutants in which a single csm gene was inactivated were created; these mutants included genes encoding all chlorosome proteins except CsmA. All mutants had BChl c contents similar to that of the wild-type strain and had growth rates indistinguishable from or within ∼90{\%} (CsmC- and CsmJ -) of those of the wildtype strain. Chlorosomes isolated from the mutants lacked only the protein whose gene had been inactivated and were generally similar to those from the wild-type strain with respect to size, shape, and BChl c, BChl a, and carotenoid contents. However, chlorosomes from the csmC mutant were about 25{\%} shorter than those from the wild-type strain, and the BChl c absorbance maximum was blue-shifted about 8 nm, indicating that the structure of the BChl c aggregates in these chlorosomes is altered. The results of the present study establish that, except with CsmA, when the known chlorosome proteins are eliminated individually, none of them are essential for the biogenesis, light harvesting, or structural organization of BChl c and BChl a within the chlorosome. These results demonstrate that chlorosomes are remarkably robust structures that can tolerate considerable changes in protein composition.",
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Nine Mutants of Chlorobium tepidum Each Unable to Synthesize a Different Chlorosome Protein Still Assemble Functional Chlorosomes. / Frigaard, Niels Ulrik; Li, Hui; Milks, Kirstin J.; Bryant, Donald Ashley.

In: Journal of bacteriology, Vol. 186, No. 3, 01.02.2004, p. 646-653.

Research output: Contribution to journalArticle

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