The 5.6-Kilodalton Protein in Isolated Chlorosomes of Chloroflexus aurantiacus Strain Ok -70-fl is a Degradation Product

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Abstract
Chlorosomcs containing BChl a790 have been isolated from Chloroflexus aurantiacus on sucrose density gradients using the detergents Miranol. Deriphat. N.N-dimethyldodecyl- aminc-N-oxidc, and dodecyl-p-D-rnaltoside. All freshly prepared samples cither lack the poly- peptide of approximately 5 kDa. which appears identical with the 5.6-kDa protein previously assigned the role of BChl c-binding [R. G. Feick and R. C. Fuller. Biochemistry 23, 3693- 3700 (1984)]. or they contain only a minor amount thereof. This polypeptide accumulates in the chlorosomcs in vitro at room temperature within 24 h after isolation. The reaction cannot be prevented simply by addition of the protease inhibitors benzamidinc. F.-caproic ac|d. and phenylmethylsulfonyl fluoride. However, upon denaturation, as required lor gel electrophore- sis, of the freshly isolated chlorosome sample the formation of the 5-kDa polypeptide is inhibit- ed. We conclude that this species, viz. 5.6-kDa protein, is a degradation product of another - as yet unidentified - protein present in the chlorosome preparations. Despite the pronounced proteolytic activity which affords the 5-kDa fragment, the native absorption and fluorescence properties of BChl c and BChl a arc essentially not changed in these chlorosome preparations.

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