1 Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.(2010)īiogenesis of membranes of plastid thylakoidsĬhlorosis, disturbed thylakoids biogenesis (2011)Ĭytoskeleton and cytoskeleton-dependent trafficking (2010)įusion of transport vesicles with cellular membrane or organelles (2012)ĭefect in leaf development and inflorescence architecture Hypocotyls and leaf development, senescence, flowering tapetum and anther developmentĭwarfness, leaves with long leafstalks, change in hypocotyl length, response to red light and darkness Slightly reduced floral organs and occasional generation of deformed petals Modulation of flowering time and flower architecture Proteolysis of proteins of circadian rhythm Loss of sensitivity to auxin, smaller number of lateral roots Proteolysis, auxin-mediated growth processes Stomatal and embryo development and stress responsesĭefects in embryo, root, seedling and stomatal development MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 4 Stem elongation, leaf development, pollen tube growth, xylem differentiation, senescence, and photomorphogenesisĭelayed growth, defects in hypocotyl, xylem cell wall, phloem differentiation, root epidermal and meristematic cell fate determination, gravitropic responses, lateral root and stomatal developmentĭefects in shoot, floral and root meristems, disturbed pollen tube elongation (2013)ĭwarfism, disoriented growth, and helical rotation of epidermal layers, reduced BR sensitivityįellerer et al. TRANSLOCON AT THE OUTER MEMBRANE OF CHLOROPLASTS 75Īronsson et al. Light intensity-dependent growth phenotype TRANSLOCON AT THE OUTER ENVELOPE MEMBRANE OF CHLOROPLASTS 64 TRANSLOCON AT THE INNER ENVELOPE MEMBRANE OF CHLOROPLASTS 40Ĭhlorosis, disrupted development of chloroplasts, delayed growth (2016)įloral patterning defects and reduced rate of leaf initiationīerardini et al. Root development, abiotic and biotic stressĭefected in R-protein-mediated resistanceĭefects in root growth, lateral root development, hypocotyl elongation and apical dominance (2017, 2018)ĬYSTEINE AND HISTIDINE-RICH DOMAIN-CONTAINING PROTEIN
#MOLECULAR CHAPERONE HUB RAR#
Protein quality control, chloroplasts biogenesisĮR-mediated stress response and thermotoleranceĭisturbed pollen germination, homeostasis of RAR (2015)įlowering, hypocotyl development and abiotic stress
Johnson and Toft (1994) D’Alessandro et al. Short root length phenotype with a reduced meristem length The function of HSP90s is considered indispensable for the maintenance of cellular homeostasis under natural growth conditions, but their activity becomes even more crucial when stress conditions compromise protein stability. The HSP90 chaperone machinery mediates the maturation of client proteins that comprise about 10–20% of the cellular proteome ( Zhao et al., 2005 Taipale et al., 2010). Co-chaperones can bind to all protein subdomains of HSP90s and this binding can be facilitated or abolished by other co-chaperones (see below) ( Table 1). Some of them affect the ATPase activity of HSP90s ( Zhang et al., 2010), while others dictate substrate specificity ( Catlett and Kaplan, 2006). These co-chaperones have diverse structure and impact HSP90 function at different stages of the chaperone cycle. HSP90s physically interact and cooperate with co-chaperones ( Table 1), which are not dependent on HSP90s to obtain and maintain their own stability.
HSP90 protein family members are expressed constitutively, and under normal conditions HSP90 protein levels represent 1–2% of the total cellular proteins, while in stress conditions, their levels rise as their transcription and translation are enhanced ( Lindquist, 1981). They function as molecular chaperones supporting the correct folding of newly synthesized proteins as well as re-folding and stabilizing tertiary structures of already folded proteins. HEAT SHOCK PROTEINS 90 (HSP90s) are evolutionarily conserved proteins found in prokaryotic and eukaryotic cells. In this concept, plants respond to moderate environmental cues by altering their transcriptional and metabolic programmes resulting in morphological changes. Plant morphogenesis is shaped by genotype, environment, and time, and these factors are intertwined in a complex regulatory network. Chaperone, client protein, co-chaperone, HEAT SHOCK PROTEIN 90, plant cell, plant development, protein kinase Introductionĭue to their sessile life style, plants possess sophisticated sensing and adaptation mechanisms that enable them to quickly respond to ever-changing environmental conditions.
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