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. 1986 Jan;80(1):231–238. doi: 10.1104/pp.80.1.231

Chlorophyll-Protein Complexes from Euglena gracilis and Mutants Deficient in Chlorophyll b1

II. Polypeptide Composition

Francis X Cunningham Jr 1,2, Jerome A Schiff 1,3
PMCID: PMC1075087  PMID: 16664588

Abstract

Chlorophyll-protein complexes (CPs) obtained from thylakoids of Euglena gracilis Klebs var bacillaris Cori contain the following polypeptides (listed in parentheses in order of prominence after Coomassie R-250 staining of polyacrylamide gels): CP Ia (66, 18, 22, 22.5, 27.5, 21, 28, 24, 25.5, and 26 kilodaltons [kD]); CP I (66 kD); CPx (41 kD); LHCP2 (an oligomer of LHCP) (26.5, 28, and 26 kD); CPy (27 and 19 kD); CPa (54 kD); and LHCP (26.5, 28, and 26 kD). Mutants of bacillaris low in chlorophyll b (Gr1BSL, G1BU, and O4BSL; Chl a/b [mol/mol] = 50-100) which lack CP Ia, LHCP2, and LHCP also lack or are deficient in polypeptides associated with these complexes in wild-type cells. Mutants G1 and O4, which also lack CPy, lack the CPy-associated polypeptides found in wild-type and Gr1. Using an antiserum which was elicited by and reacts strongly and selectively with the SDS-treated major polypeptide (26.5 kD) of the LHCP complexes of wild-type, this polypeptide is undetectable in the mutants (≪0.25% of the level in wild-type on a cell basis); the antiserum does not react with the SDS-treated 28 kD polypeptide of the Euglena LHCP complexes and cross-reacts only very weakly with components in SDS-treated cells of Chlamydomonas reinhardtii Dangeard and chloroplasts of Spinacia oleracea L. cv Winter Bloomsdale. Rates of photosynthesis of the wild-type and mutant cells of Euglena are approximately equal on a cell basis when measured at light saturation, consistent with the selective loss of major antenna components but not CP I or CPa from the mutants.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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