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)

Autor:	Peter Beyer, Monier H. Tadros, Salim Al-Babili, Joël Vandekerckhove, M. Bonk
Rok vydání:	1996
Předmět:	Phytoene desaturase Physiology food and beverages Plant Science Biology Hsp70 chemistry.chemical_compound Biosynthesis chemistry Biochemistry Heat shock protein Chaperone (protein) Chromoplast Genetics biology.protein Plastid Flower formation
Zdroj:	Plant Physiology. 111:931-939
ISSN:	1532-2548 0032-0889
DOI:	10.1104/pp.111.3.931
Popis:	In chromoplast differentiation during flower formation in Narcissus pseudonarcissus, the molecular chaperones chaperonin 60 (Cpn60; α- 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::fb927b76f85aa57b17c6695492a32d1d https://doi.org/10.1104/pp.111.3.931 Zobrazit plný text záznamu