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- 저자 : Jane Waters (검색결과 2 건)
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Risk-Taking in the New Zealand Bush: Issues of Resilience and Wellbeing
Amanda Bateman,Jane Waters 환태평양유아교육연구학회 2018 Asia-Pacific journal of research in early childhoo Vol.12 No.2
This article discusses a single case analysis of teacher-child interactions on an everyday bush walk in New Zealand. It uses a combination of the Leuven wellbeing scale (Laevers, 2000) and a conversation analysis approach to explore how children and teachers attend to specific features of the outdoor environment in a way that encourages risk-taking and builds resilience through problem solving. The collaborative achievement of the activities between the pre- school teacher and the fouryear-old children are discussed as an important and necessary aspect of the interactions, which we suggest may represent physical sustained shared thinking, for supporting wellbeing whilst building resilience and risk-taking. Implications for future practice are considered with regard to implementation of early childhood curricula.
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The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and chloroplast development
Lee, Ung,Rioflorido, Ignatius,Hong, Suk-Whan,Larkindale, Jane,Waters, Elizabeth R.,Vierling, Elizabeth Blackwell Publishing Ltd 2007 The Plant journal Vol.49 No.1
<P>Summary</P><P> The Casein lytic proteinase/heat shock protein 100 (Clp/Hsp100) proteins are chaperones that act to remodel/disassemble protein complexes and/or aggregates using the energy of ATP. In plants, one of the best-studied proteins from this family is cytosolic ClpB1 (At1g74310), better known in Arabidopsis as <I>At</I>Hsp101, which is a heat shock protein required for acclimation to high temperatures. Three other ClpB homologues have been identified in the Arabidopsis genome (ClpB2, ClpB3 and ClpB4; At4g14670, At5g15450 and At2g25140). To define further the roles of these chaperones in plants we investigated their intracellular localization, evolutionary relationships, patterns of expression and the phenotypes of corresponding T-DNA insertion mutants. We first found that ClpB2 was misannotated; there is no functional ClpB/Hsp100 gene at this locus. By fusing the putative transit peptides of ClpB3 and ClpB4 with GFP, we showed that these proteins are targeted to the chloroplast and mitochondrion, respectively, and we therefore designated them as ClpB-p and ClpB-m. Phylogenetic analysis supports two major lineages of ClpB proteins in plants, an ‘eukaryotic’, cytosol/nuclear-localized group containing <I>At</I>Hsp101, and an organelle-localized lineage, containing both ClpB-p and ClpB-m. Although <I>At</I>Hsp101, ClpB-p and ClpB-m transcripts all accumulate dramatically at high temperatures, the T-DNA insertion mutants of ClpB-p and ClpB-m show no evidence of seedling heat stress phenotypes similar to those observed in <I>At</I>Hsp101 mutants. Strikingly, ClpB-p knockouts were seedling lethals, failing to accumulate chlorophyll or properly develop chloroplasts. Thus, in plants, the function of ClpB/Hsp100 proteins is not restricted to heat stress, but a specific member of the family provides housekeeping functions that are essential to chloroplast development.</P>
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