The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin

Li, Hao; Yu, Ying-ying; Ruan, Meixia; Jiao, Fang; Chen, Hailong; Gao, Jiali; Bao, Yongzhen; Weng, Yuxiang

doi:10.1016/j.bpj.2022.05.032

Cited by 5 publications

(6 citation statements)

References 83 publications

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“…The secondary structure of OsCIPK7 shifts at different temperatures (Zhang et al , 2019a ). Thus, to analyze whether cold stress alters the secondary structure of OsCRT3, Fourier‐transform infrared (FTIR) spectroscopy assays were conducted (Li et al , 2020a , 2022 ). The secondary derivative spectra with the typical absorption peaks were denoted together with their assignments.…”

Section: Resultsmentioning

confidence: 99%

“…The EMBO Journal 42: e110518 | 2023 secondary structure of OsCRT3, Fourier-transform infrared (FTIR) spectroscopy assays were conducted (Li et al, 2020a(Li et al, , 2022. The secondary derivative spectra with the typical absorption peaks were denoted together with their assignments.…”

Section: ó2022 the Authorsmentioning

confidence: 99%

“…Fourier transform infrared (FTIR) assay FTIR spectroscopy was performed as described (Li et al, 2020a(Li et al, , 2022. The OsCRT3 protein or RGA1 protein was freeze-dried through a vacuum at À10°C for lyophilization, and then the lyophilized proteins were dissolved in PBS buffer (50 mM K 2 DPO 4 / KD 2 PO 4 , pH7.4) containing 99.9% D 2 O. FTIR absorption spectra at different temperatures were acquired on a spectrometer (VERTEX 70 V, Bruker Optics, Madison, WI, USA).…”

Section: Luciferase Complementation Imaging Assay (Lci)mentioning

confidence: 99%

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Cold‐induced calreticulin OsCRT3 conformational changes promote OsCIPK7 binding and temperature sensing in rice

et al. 2022

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Unusually low temperatures caused by global climate change adversely affect rice production. Sensing cold to trigger signal network is a key base for improvement of chilling tolerance trait. Here, we report that Oryza sativa Calreticulin 3 (OsCRT3) localized at the endoplasmic reticulum (ER) exhibits conformational changes under cold stress, thereby enhancing its interaction with CBL-interacting protein kinase 7 (OsCIPK7) to sense cold. Phenotypic analyses of OsCRT3 knock-out mutants and transgenic overexpression lines demonstrate that OsCRT3 is a positive regulator in chilling tolerance. OsCRT3 localizes at the ER and mediates increases in cytosolic calcium levels under cold stress. Notably, cold stress triggers secondary structural changes of OsCRT3 and enhances its binding affinity with OsCIPK7, which finally boosts its kinase activity. Moreover, Calcineurin B-like protein 7 (OsCBL7) and OsCBL8 interact with OsCIPK7 specifically on the plasma membrane. Taken together, our results thus identify a cold-sensing mechanism that simultaneously conveys cold-induced protein conformational change, enhances kinase activity, and Ca 2+ signal generation to facilitate chilling tolerance in rice.

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Section: Resultsmentioning

confidence: 99%

Section: ó2022 the Authorsmentioning

confidence: 99%

Section: Luciferase Complementation Imaging Assay (Lci)mentioning

confidence: 99%

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Cold‐induced calreticulin OsCRT3 conformational changes promote OsCIPK7 binding and temperature sensing in rice

et al. 2022

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“…Another pathway to suppress protein aggregation is to employ the chaperone protein and hence inflate the degradation mechanism. 9,13,14 Several studies have been carried out for the development of antiamyloidogenic agents, especially for proteins and peptides related to amyloids for both in vitro and in vivo conditions. 15−19 Various polyphenols have been reported as attractive candidates for inhibiting the β-amyloid fibrils.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Presently, for the treatment of the amyloid-associated disorders, many therapeutic strategies have been proposed, including protein mutagenesis and control on protein concentration, pH, and temperature with emphasis on the distortion of the fibrillar structures of the protein. , These therapies focus on the roots of the pathological disease with the ultimate objective of curing them. Another pathway to suppress protein aggregation is to employ the chaperone protein and hence inflate the degradation mechanism. ,, …”

Section: Introductionmentioning

confidence: 99%

Cholinium-Based Ionic Liquids Attenuate the Amyloid Fibril Formation of Lysozyme: A Greener Concept of Antiamyloidogenic Ionic Liquids

Sindhu

Varma

Venkatesu

2022

ACS Sustainable Chem. Eng.

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Amyloid fibrils share dominant β-sheet structures that form pathological deposits in human organs causing various debilitating neurodegenerative diseases such as type II diabetes, Huntington's, Alzheimer's, and Parkinson's diseases, and thus, the treatment of these amyloid-based diseases is a major overriding concern. Ionic liquids (ILs), being biocompatible solvent medium for proteins, have been introduced as effective antiamyloidogenic agents to prevent the fibrillation process; bio-derived choliniumbased ILs ([Chn] ILs) deserve special attention in view of their inhibitory action on protein amyloid formation to enable the restoration of its biochemical function. Herein, the antiamyloidogenic action of four [Chn] ILs, namely cholinium acetate, and cholinium dihydrogen phosphate [Chn][Dhp], on the in vitro amyloid formation of the lysozyme (Lys) was investigated by applying ThT fluorescence, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectroscopy. Additionally, transmission electronic microscopy (TEM), dynamic light scattering (DLS), and atomic force microscopy (AFM) measurements were also performed to ascertain the morphological changes. Interestingly, with incubation of Lys without ILs there was a substantial increase in thioflavin T (ThT) fluorescence intensity for the Lys, confirming the formation of Lys fibrillar aggregates. The results of FT-IR and UV-CD measurements showed that the Lys secondary structure was retained in the presence of the [Chn][Bit] and [Chn][DHP] ILs, which was lost in the absence of these ILs in the incubating conditions. It was further inferred by morphological analysis via TEM, AFM, and DLS that through thermochemical treatment of Lys, fibrils were formed, and these [Chn] ILs exhibit an increased propensity to suppress the formation of mature fibrils. Overall, the inhibition efficiency of these [Chn] ILs is accredited to the bio-derived cholinium cations as well as the nature of anions based on Hofmeister series. The present study offers a deep insight into the role of ILs in controlling the fibril formation in proteins and thus, they may serve as agents to remediate neurodegenerative diseases.

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A neutral invertase controls cell division besides hydrolysis of sucrose for nutrition during germination and seed setting in rice

Wang,

Li,

Weng

2024

iScience

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The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin

Cited by 5 publications

References 83 publications

Cold‐induced calreticulin OsCRT3 conformational changes promote OsCIPK7 binding and temperature sensing in rice

Cold‐induced calreticulin OsCRT3 conformational changes promote OsCIPK7 binding and temperature sensing in rice

Cholinium-Based Ionic Liquids Attenuate the Amyloid Fibril Formation of Lysozyme: A Greener Concept of Antiamyloidogenic Ionic Liquids

A neutral invertase controls cell division besides hydrolysis of sucrose for nutrition during germination and seed setting in rice

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