Characterization of a cDNA encoding for the 28.5-kDa LHCII apoprotein from the unicellular marine chlorophyte, Dunaliella tertiolecta

Julie LaRoche, John Bennett, Paul G. Falkowski

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Résumé

Three distinct clones, encoding light-harvesting chlorophyll (LHCII) proteins associated with photosystem II were isolated from a cDNA library of the unicellular marine chlorophyte, Dunaliella tertiolecta. We determined the nucleotide sequence of one of these clones, as well as the N-terminal amino acid (aa) sequences of the four mature LHCII apoproteins (24.5, 28.5, 30 and 31 kDa). The sequenced cDNA clone encoded the precursor of the 28.5-kDa apoprotein. We deduced that the transit peptide is 30 aa long and the mature protein is processed between A and V within the peptide RAAVEFYGP. Southern blots of D. tertiolecta genomic DNA indicated the presence of three to five genes. The algal aa sequence differs from higher plants mainly in the transit peptide and the N terminus. Several aa residues, highly conserved in higher plants, which are believed to play a role in chlorophyll binding, are not conserved in the chlorophytes.

Langue d'origineEnglish
Pages (de-à)165-171
Nombre de pages7
JournalGene
Volume95
Numéro de publication2
DOI
Statut de publicationPublished - nov. 15 1990
Publié à l'externeOui

Note bibliographique

Funding Information:
We wish to thank Drs. K. Cone and B. Burr for technical advice in constructing the eDNA library and for discussions, Dr. G. Schmidt for providing the LHCII probes from Chlamydomonaansd, Dr. C.W. Anderson and Ms. J.R. Wysocki for the aa sequencing. Dr. R. Herzig isolated the LHCII complex used for the aa microsequencing. We are indebted to Mr. K. Wyman for technical help. This research was supported by the U.S. Department of Energy, Office of Basic Biological Energy Sciences. This research was performed under the auspices of the United States Department of Energy under Contract no. DE-AC02-76CH00016.

ASJC Scopus Subject Areas

  • Genetics

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