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Plant and Cell Physiology, 1995, Vol. 36, No. 8 1483-1492
© 1995

Localization and Characterization of a Novel 20 kDa Polypeptide in the Chloroplast of the Green Alga Dunaliella salina

Eva Andreasson1 and Anastasios Melis2

Department of Plant Biology, 411 Koshland Hall, University of California Berkeley, CA 94720-3102, U.S.A.

2To whom correspondence should be addressed.

Recent work with the green alga Dunaliella salina showed the presence of a {small tilde}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 {small tilde}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 {small tilde}20 kDa polypeptide is easily degraded to a {small tilde}19 kDa product during sample preparation. A limited amino acid sequence of 21 residues from the free N-terminus of the {small tilde}19 kDa product was obtained. On the basis of this partial sequence, it was concluded that the {small tilde}20 kDa polypeptide is not a degradation product of a known LHC-II but rather a novel protein. The {small tilde}20kDa 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 {small tilde}20 kDa polypeptide is not an ELIP (early light-inducible protein). Possible functions of the {small tilde}20 kDa protein are discussed.

1Permanent address: Department of Biochemistry, University of lund, PO Box 124, S-221 00 Lund, Sweden

(Received July 12, 1995; Accepted August 29, 1995)
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