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Mini Review

Staying in the fold: The SGT1/chaperone machinery in maintenance and evolution of leucine-rich repeat proteins

Johannes Stuttmann , Jane E. Parker and Laurent D. Noël

volume 3 | issue 5

may 2008
Pages: 283 - 285

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The conserved eukaryotic protein SGT1 (Suppressor of G2 allele of skp1) participates in diverse physiological processes such as cell cycle progression in yeast, plant immunity against pathogens and plant hormone signalling. Recent genetic and biochemical studies suggest that SGT1 functions as a novel co-chaperone for cytosolic/nuclear HSP90 and HSP70 molecular chaperones in the folding and maturation of substrate proteins. Since proteins containing the leucine-rich repeat (LRR) protein-protein interaction motif are overrepresented in SGT1-dependent phenomena, we consider whether LRR-containing proteins are preferential substrates of an SGT1/HSP70/HSP90 complex. Such a chaperone organisation is reminiscent of the HOP/HSP70/HSP90 machinery which controls maturation and activation of glucocorticoid receptors in animals. Drawing on this parallel, we discuss the possible contribution of an SGT1-chaperone complex in the folding and maturation of LRR-containing proteins and its evolutionary consequences for the emergence of novel LRR interaction surfaces.

Authors

Johannes Stuttmann

Laboratoire de Biologie du Développement des Plantes; IBEB/SBVME; UMR 6191 CNRS-CEA-Université de la méditerranée Aix-Marseille II; CEN Cadarache; Saint Paul-lez-Durance; France

Jane E. Parker

Department of Plant-Microbe Interactions; Max-Planck Institute for Plant Breeding Research; Köln, Germany

Laurent D. Noël

Laboratoire des interactions plantes-microorganismes; UMR2594 CNRS-INRA; Chemin de Borde-Rouge; BP 52627; Castanet-Tolosan, France