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PLANT PHYSIOLOGY , Vol 111, Issue 3 931-939, Copyright © 1996 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Purification and Characterization of Chaperonin 60 and Heat-Shock Protein 70 from Chromoplasts of Narcissus pseudonarcissus (Involvement of Heat-Shock Protein 70 in a Soluble Protein Complex Containing Phytoene Desaturase)
M. Bonk, M. Tadros, J. Vandekerckhove, S. Al-Babili and P. Beyer
Institut fur Biologie II der Universitat, Zellbiologie (M.B., S.A.-B., P.B.), and Institut fur Biologie II der Universitat, Mikrobiologie (M.T.), Schanzlestrasse 1, D-79104 Freiburg, Germany
In chromoplast differentiation during flower formation in Narcissus
pseudonarcissus, the molecular chaperones chaperonin 60 (Cpn60; [alpha] and
[beta]) and heat-shock protein 70 (Hsp70) greatly increase in abundance.
Both were purified and shown to be present in a functional form in
chromoplasts, indicating their requirement in the extensive structural
rearrangements during the chloroplast-to-chromoplast transition. The
purified proteins, sequenced N terminally and from internal peptides,
showed strong homology to plastid Cpn60 and Hsp70 representatives from
other plant species. During chromoplast differentiation, the carotenoid
biosynthetic pathway is strongly induced. The corresponding enzymes are all
nuclear encoded and form a large, soluble, hetero-oligomeric protein
complex after import but prior to their membrane attachment. By
immunoprecipitations we have shown that the plastid Hsp70 is a structural
constituent of a soluble entity also containing phytoene desaturase.
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