You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
psbA in the Marine Chromophyte Heterosigma carterae: Evolutionary Analysis and Comparative Structure of the D1 Carboxyl Terminus
Linda K. Hardison, Barbara A. Boczar and Rose Ann Cattolico
American Journal of Botany
Vol. 82, No. 7 (Jul., 1995), pp. 893-902
Published by: Botanical Society of America, Inc.
Stable URL: http://www.jstor.org/stable/2445976
Page Count: 10
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
The 32 kDa D1 protein, encoded by the psbA gene, is a component of photosystem II in photosynthetic eukaryotes and cyanobacteria. In the chl a,c-containing alga Heterosigma carterae (previously referred to as Olisthodiscus luteus), psbA is transcribed as a 1.7-kb monocistronic message. The transcription start site and putative prokaryotic-like -10 (TATAAT) and -35 (GTGATT) promoter domains have been identified for this gene, which encodes a protein that is 360 amino acids in length. The protein contains a seven amino acid motif near the carboxyl terminus that is also present in non-chl b-containing algal plastids and cyanobacteria, but not in terrestrial plants, green algae, or the prokaryote Prochlorothrix. Phylogenetic analysis of D1 sequences, with special attention to the seven amino acid motif, suggests that plastids of rhodophytic and chromophytic algae form an evolutionary lineage distinct from cyanobacteria and chlorophytic (chl a,b-containing) chloroplasts. A model for the function of the seven amino acid motif is proposed.
American Journal of Botany © 1995 Botanical Society of America, Inc.