Molecular Chaperone: Structure, Function, and Role in Plant Abiotic Stress Tolerance

Trivedi, Dipesh Kumar; Huda, Kazi Md. Kamrul; Gill, Sarvajeet Singh; Tuteja, Narendra

doi:10.1002/9783527694570.ch7

Cited by 7 publications

(5 citation statements)

References 114 publications

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“…They are responsible for the transport of proteins in different cellular organelles and in translocating misfolded proteins toward the UPS for deterioration. They are also involved in the transport of many transmembrane proteins, aids in their folding, and protect them from stressful conditions (Trivedi et al, 2016). The identification of HSP70 in our study indicates their involvement in the translocation of misfolded and other functional proteins toward their target site to maintain cellular homeostasis in normal and stressful conditions.…”

Section: Transport Related Proteinsmentioning

confidence: 59%

“…The failure can lead to the death of a new plant. Chaperones protect the proteins in their functionally active form and are concerned with assembly, folding and sustainability, and proteolysis (Trivedi et al, 2016). In this study, we identified 53 defense-related proteins (Table 3) corresponding to 9% of the total identified proteins.…”

Section: Proteostasis and Defense Related Proteinsmentioning

confidence: 99%

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Proteomic Analysis of Embryo Isolated From Mature Jatropha curcas L. Seeds

et al. 2022

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Jatropha curcas L. is a non-edible oilseed containing almost 40% of seed oil and is famous as the best source of raw material for biofuel production. J. curcas seeds contain three main tissues, such as inner integument, endosperm, and embryo. To best understand the physiological events related to specific tissues, it is important to perform the proteome analysis of these tissues. Previously we have explored the pattern of reserves deposition and tissue-specific biological pathways by analyzing the proteome of the inner integument and endosperm and organelles, such as plastids and gerontoplasts isolated from these tissues. The focus of the present study was to perform the proteomic analysis of embryo isolated from the mature seeds of J. curcas. This analysis resulted in the identification of 564 proteins of which 206 are not identified previously from any other tissue of this plant. The identified proteins were functionally classified using the MapMan classification system revealing various proteins involved in different functionalities. The proteins involved in transport functions and those with proteolytic activity were determined through the Transporter Classification Database (TCDB) and MEROPS database, respectively. In addition to identify a large number of proteins participating in various metabolic processes, we found several proteins involved in defense functions, such as the members of chaperones and the ubiquitin-proteasome system. Similarly, members of the legumin and vicilin family of seed storage proteins (SSPs) were identified which in addition to their storage function, are involved in defense. In addition, we have reported that proteases belonging to different mechanistic classes and are involved in diverse physiological functions. Last but not the least, several classes of transport-related proteins were identified that are discussed concerning their function in the transportation of different nutrients across the embryo. To the best of our knowledge, this study reported the highest number of proteins identified from the embryo of mature J. curcas seeds, most of which are essential for seed germination, reflecting the fact that many proteins required for germination are already present in the mature embryo.

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Section: Transport Related Proteinsmentioning

confidence: 59%

Section: Proteostasis and Defense Related Proteinsmentioning

confidence: 99%

Proteomic Analysis of Embryo Isolated From Mature Jatropha curcas L. Seeds

et al. 2022

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“…It is reported that HSP60 has a 15-30% contribution in cellular protein folding and maintenance and also plays a vital role in mitochondrial protein transportation (Trivedi et al 2016). In addition, the elevated expression level of HSP/molecular chaperones assist in the assembly of the highly abundant secretory storage proteins in the endoplasmic reticulum lumen during seed development (Trivedi et al 2016). Taken together, that may be why there is a high abundance of GroEL chaperones in seed storage proteins.…”

Section: Discussionmentioning

confidence: 99%

Structure and function of seed storage proteins in faba bean (Vicia faba L.)

Liu

Hou

et al. 2017

3 Biotech

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The protein subunit is the most important basic unit of protein, and its study can unravel the structure and function of seed storage proteins in faba bean. In this study, we identified six specific protein subunits in Faba bean (cv. Qinghai 13) combining liquid chromatography (LC), liquid chromatography-electronic spray ionization mass (LC-ESI-MS/MS) and bio-information technology. The results suggested a diversity of seed storage proteins in faba bean, and a total of 16 proteins (four GroEL molecular chaperones and 12 plant-specific proteins) were identified from 97-, 96-, 64-, 47-, 42-, and 38-kD-specific protein subunits in faba bean based on the peptide sequence. We also analyzed the composition and abundance of the amino acids, the physicochemical characteristics, secondary structure, three-dimensional structure, transmembrane domain, and possible subcellular localization of these identified proteins in faba bean seed, and finally predicted function and structure. The three-dimensional structures were generated based on homologous modeling, and the protein function was analyzed based on the annotation from the non-redundant protein database (NR database, NCBI) and function analysis of optimal modeling. The objective of this study was to identify the seed storage proteins in faba bean and confirm the structure and function of these proteins. Our results can be useful for the study of protein nutrition and achieve breeding goals for optimal protein quality in faba bean.

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“…Anggota famili ini berfungsi sebagai molekular chaperone untuk protein yang baru disintesis untuk mencegah akumulasi protein yang berlebih dan memastikan folding protein yang benar selama proses transfer protein ke sel target (Su & Li, 2008). Selain itu, HSP70 berperan untuk menentukan daerah membran yang tepat untuk mentranslokasikan protein-protein yang ada pada organisme dan degradasi protein yang gagal mengalami pelipatan (Trivedi et al, 2016). HSP70 juga memiliki fungsi lain yaitu mengikat dan menstabilkan polipeptida dari ribosom dan menstranslokasikan protein melewati membran ke retikulum endoplasma atau mitokondria.…”

Section: Hsp70unclassified

Peran Chaperone Pada Tumbuhan: Mini Review

2019

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Plants respond to various conditions in the surrounding environment, whether favorable conditions or vice versa. Abiotic and biotic factors affect plant responses such as temperature, humidity, salinity, insects and pathogens such as viruses and bacteria. Plants have a defense system in tolerancing stress from the surrounding environment, for example heat shock protein (HSP) is a chaperone protein that plays a role in plant defenses when experiencing stress to the temperature. HSP is classified into six families based on their molecular weight, namely HSP100, HSP90, HSP70, HSP60, HSP40, and small HSP. Each has a role in maintaining the stability of plant metabolism. HSP is especially important for correct protein refolding, preventing degradation and denaturation of protein. Key words: plants; chaperone; heat shock protein; refolding; protein denaturation.

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Molecular Chaperone: Structure, Function, and Role in Plant Abiotic Stress Tolerance

Cited by 7 publications

References 114 publications

Proteomic Analysis of Embryo Isolated From Mature Jatropha curcas L. Seeds

Proteomic Analysis of Embryo Isolated From Mature Jatropha curcas L. Seeds

Structure and function of seed storage proteins in faba bean (Vicia faba L.)

Peran Chaperone Pada Tumbuhan: Mini Review

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