Functional characterization of orchardgrass endoplasmic reticulum-resident Hsp90 (DgHsp90) as a chaperone and an ATPase

Yung, Joon; Jung, Mi; Ermawati, Netty; Su’udi, Mukhamad; Rho, Gyu Jin; Han, Chang‐deok; Lee, Kon Ho; Son, Daeyoung

doi:10.1016/j.plaphy.2009.06.008

Cited by 15 publications

(11 citation statements)

References 36 publications

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“…To determine if NCA1 has holdase chaperone activity that effectively maintains nascent chains in a folding-competent conformation, the holdase activity of His-NCA1 was assayed by measuring its capacity to suppress thermal aggregation of Arabidopsis malate dehydrogenase (MDH, EC 1.1.1.37; a model substrate for holdase assay, as described in Cha et al, 2009). MDH aggregation was monitored by measuring absorbance at 340 nm without or with NCA1 under thermal denaturing conditions at 45°C.…”

Section: Nca1 Has Chaperone Protein Activitymentioning

confidence: 99%

“…Arabidopsis MDH (EC 1.1.1.37) and HSP90.2 were prepared as described previously (Cha et al, 2009;Kim et al, 2011). The proteins were further dialyzed against 50 mM Tris-HCl, pH 8.0.…”

Section: Holdase Chaperone Assaymentioning

confidence: 99%

“…The proteins were further dialyzed against 50 mM Tris-HCl, pH 8.0. Holdase chaperone activity of His-NCA1 was assayed by measuring its capacity to suppress thermal aggregation of MDH or His-CAT2, as described by Cha et al (2009). MDH or CAT2 aggregation was monitored in reaction buffer (40 mM HEPES, pH 7.5) by measuring absorbance at 340 nm using a Beckman DU-800 spectrophotometer attached to a thermostatic cell holder assembly at 45°C.…”

Section: Holdase Chaperone Assaymentioning

confidence: 99%

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A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis

et al. 2015

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Catalases are key regulators of reactive oxygen species homeostasis in plant cells. However, the regulation of catalase activity is not well understood. In this study, we isolated an Arabidopsis thaliana mutant, no catalase activity1-3 (nca1-3) that is hypersensitive to many abiotic stress treatments. The mutated gene was identified by map-based cloning as NCA1, which encodes a protein containing an N-terminal RING-finger domain and a C-terminal tetratricopeptide repeat-like helical domain. NCA1 interacts with and increases catalase activity maximally in a 240-kD complex in planta. In vitro, NCA1 interacts with CATALASE2 (CAT2) in a 1:1 molar ratio, and the NCA1 C terminus is essential for this interaction. CAT2 activity increased 10-fold in the presence of NCA1, and zinc ion binding of the NCA1 N terminus is required for this increase. NCA1 has chaperone protein activity that may maintain the folding of catalase in a functional state. NCA1 is a cytosol-located protein. Expression of NCA1 in the mitochondrion of the nca1-3 mutant does not rescue the abiotic stress phenotypes of the mutant, while expression in the cytosol or peroxisome does. Our results suggest that NCA1 is essential for catalase activity.

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Section: Nca1 Has Chaperone Protein Activitymentioning

confidence: 99%

“…Arabidopsis MDH (EC 1.1.1.37) and HSP90.2 were prepared as described previously (Cha et al, 2009;Kim et al, 2011). The proteins were further dialyzed against 50 mM Tris-HCl, pH 8.0.…”

Section: Holdase Chaperone Assaymentioning

confidence: 99%

Section: Holdase Chaperone Assaymentioning

confidence: 99%

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A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis

et al. 2015

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“…Zhang et al [78] cloned four classes of HSPs (HSP100, HSP90, HSP70, and sHSPs) that are differentially expressed under heat stress between the two genotypes of fescues, which are widely used as both forage and turf grasses. Cha et al [80] characterized an endoplasmic reticulum-resident HSP90 gene from orchard grass, whose expression increased during heat stress. This protein functions as a molecular chaperone by preventing thermal aggregation of malate dehydrogenase and citrate synthase.…”

Section: Identification and Characterization Of Hsps Associated Wimentioning

confidence: 99%

Heat Shock Proteins in Association with Heat Tolerance in Grasses

Zhan

Huang

2011

International Journal of Proteomics

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The grass family Poaceae includes annual species cultivated as major grain crops and perennial species cultivated as forage or turf grasses. Heat stress is a primary factor limiting growth and productivity of cool-season grass species and is becoming a more significant problem in the context of global warming. Plants have developed various mechanisms in heat-stress adaptation, including changes in protein metabolism such as the induction of heat shock proteins (HSPs). This paper summarizes the structure and function of major HSPs, recent research progress on the association of HSPs with grass tolerance to heat stress, and incorporation of HSPs in heat-tolerant grass breeding.

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“…These proteins can be found in the cytosol, nucleoplasm, endoplasmic reticulum (ER), mitochondria and chloroplasts (Csermely et al , 1998; Felts et al , 2000; Krishna & Gloor, 2001). HSP90s contain three functional domains, a nucleotide binding domain of c. 25 kDa, a substrate binding domain of c. 35 kDa and a dimerization domain of c. 10 kDa in the N‐terminal, central and C‐terminal regions, respectively (Stebbins et al , 1997; Cha et al , 2009). These domains are highly conserved among HSP90 family members.…”

Section: Introductionmentioning

confidence: 99%

Expression pattern of heat shock protein 90 gene of humphead snapper Lutjanus sanguineus during pathogenic Vibrio harveyi stress

Zhang

Dai

et al. 2011

Journal of Fish Biology

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The full-length cDNA of heat shock protein 90 (HSP90) of humphead snapper Lutjanus sanguineus, designated as rsHSP90, was cloned by rapid amplification of complementary (c)DNA ends (RACE) techniques with the primers designed from the known expressed sequence tag (EST) sequence identified from the subtracted cDNA library of the head kidney of L. sanguineus. Sequence analysis showed that the full-length cDNA of rsHSP90 was 2745 bp, containing a 5' terminal untranslated region (UTR) of 99 bp, a 3' terminal UTR of 471 bp and an open reading frame (ORF) of 2175 bp encoding a polypeptide of 725 amino acids. On the basis of the deduced amino acid sequence, the theoretical molecular mass of rsHSP90 was calculated to be 83·18 kDa with an isoelectric point of 4·79. Moreover, five classical HSP90 family signatures were found in the amino acids sequence of rsHSP90 by PredictProtein. Basic local-alignment search-tool (BLAST) analysis revealed that the amino acids sequence of rsHSP90 had the highest similarity of 97% when compared with other HSP90s. Fluorescent real-time quantitative reverse-transcription (RT)-PCR was used to examine the expression pattern of rsHSP90 in eight kinds of tissues and organs of L. sanguineus challenged with Vibrio harveyi. There was a clear time-dependent expression pattern of rsHSP90 in head kidney, spleen and thymus after bacterial challenge and the expression of messenger (m)RNA reached the maximum level at the time points of 9, 15 and 24 h, respectively. The up-regulated mRNA expression of rsHSP90 in L. sanguineus after bacterial challenge indicated that rsHSP90 was inducible and might be involved in immune response.

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Functional characterization of orchardgrass endoplasmic reticulum-resident Hsp90 (DgHsp90) as a chaperone and an ATPase

Cited by 15 publications

References 36 publications

A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis

A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis

Heat Shock Proteins in Association with Heat Tolerance in Grasses

Expression pattern of heat shock protein 90 gene of humphead snapper Lutjanus sanguineus during pathogenic Vibrio harveyi stress

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