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Gene for the Ribulose-1,5-bisphosphate Carboxylase Small Subunit Protein of the Marine Chromophyte Olisthodiscus luteus is Similar to that of a Chemoautotrophic Bacterium
Barbara A. Boczar, Terrence P. Delaney and Rose Ann Cattolico
Proceedings of the National Academy of Sciences of the United States of America
Vol. 86, No. 13 (Jul. 1, 1989), pp. 4996-4999
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/34032
Page Count: 4
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The photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase [3-phospho-D-glycerate carboxylyase (dimerizing), EC 22.214.171.124] small subunit protein is encoded by the gene rbcS in the chloroplast genome of the unicellular alga Olisthodiscus luteus. This observation contrasts sharply with that seen in terrestrial plants and green algae, where rbcS is nuclear-localized. In this study, the O. luteus rbcS gene has been sequenced. The predicted primary structure of the protein sequence is 139 amino acids in length and lacks an N-terminal signal sequence. Unexpectedly, the O. luteus rbcS amino acid sequence shows the greatest similarity (56% identity) to that of the chemolithotrophic bacterium Alcaligenes eutrophus. A comparison of the N-terminal amino acid rbcS sequence of A. eutrophus to those of O. luteus and brown alga Fucus species shows extensive sequence similarity (68.3% identity). This observation suggests that the rbcS genes of these organisms are evolutionary homologues and may provide useful information in the study of small-subunit function.
Proceedings of the National Academy of Sciences of the United States of America © 1989 National Academy of Sciences