作者: Raphael Trösch , Michael Schroda , Felix Willmund
DOI: 10.1007/978-1-4939-1136-3_13
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摘要: Molecular chaperones play essential roles in a wide variety of cellular processes, from de-novo protein folding to disaggregation under stress conditions, unfolding and re-folding misfolded proteins, degradation, transport proteome remodeling during development. Almost all cell compartments contain chaperone activity some extent, hence it is not surprising that large number also the plastid compartment. Here, focus on targeting (protein import assembly complexes target membranes) as well protection specific chloroplast-derived stresses. Moreover, important plastid-encoded soluble proteins after processing transit peptides, degradation. The four major groups molecular chaperones, chaperonin/Cpn60, Hsp70, Hsp90 Hsp100 families are present plastids but many cofactors co-chaperones have yet been identified. Although function generally conserved, seems plastid-localized evolved functions mechanisms. Current research focuses therefore specificities context their environment requirements.