Localization and Characterization of a Novel 20 kDa Polypeptide in the Chloroplast of the Green Alga Dunaliella salina : MEMBRANES AND BIOENERGETICS: STRUCTURE AND FUNCTION OF CELLS

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Recent work with the green alga Dunaliella salina showed the presence of a 〜20 kDa chloroplast protein that was recognized by polyclonal antibodies raised against the isolated LHC-II [Webb M.R. and Melis A. (1995) Plant Physiol. 107: 885]. In this report, a characterization of the 〜20 kDa polypeptide is presented. It is shown that it is localized in the chloroplast envelope membrane of D. salina. The abundance of this protein is constant on a per cell basis and independent of the light regime during cell growth. The 〜20 kDa polypeptide is easily degraded to a 〜19 kDa product during sample preparation. A limited amino acid sequence of 21 residues from the free N-terminus of the 〜19 kDa product was obtained. On the basis of this partial sequence, it was concluded that the 〜20 kDa polypeptide is not a degradation product of a known LHC-II but rather a novel protein. The 〜20 kDa polypeptide did not cross-react with antibodies raised against the Cbr (carotene biosynthesis-related) gene product and showed a different electrophoretic mobility from the latter. Light-shift experiments suggest that the 〜20 kDa poly-peptide is not an ELIP (early light-inducible protein). Possible functions of the 〜20 kDa protein are discussed.
日本植物生理学会の論文