Chaperone function of two small heat shock proteins from maize

Klein, Roger D.; Chidawanyika, Tamutenda; Tims, Hannah S.; Meulia, Tea; Bouchard, Robert A.; Pett, Virginia B.

doi:10.1016/j.plantsci.2014.01.012

Cited by 17 publications

(12 citation statements)

References 69 publications

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“…Hence, this protein was possibly degraded after camphor inhibition to limit water loss, and therefore, the tubers retained more moisture compared to the sprouting tuber ( Figure 1 C). Heat shock protein HSP20s assisted protein folding and maintained protein function stability under abiotic stress, participating in folding, transport and assembly of nascent polypeptide [ 45 ]. During tuber sprouting, increasing transcript and decreasing protein abundance of HSP20s may be caused by low translation efficiency or protein degradation.…”

Section: Discussionmentioning

confidence: 99%

Comparative Morphology, Transcription, and Proteomics Study Revealing the Key Molecular Mechanism of Camphor on the Potato Tuber Sprouting Effect

Xue

Deng

et al. 2017

IJMS

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Sprouting regulation in potato tubers is important for improving commercial value and producing new plants. Camphor shows flexible inhibition of tuber sprouting and prolongs the storage period of potato, but its underlying mechanism remains unknown. The results of the present study suggest that camphor inhibition caused bud growth deformities and necrosis, but after moving to more ventilated conditions, new sprouts grew from the bud eye of the tuber. Subsequently, the sucrose and fructose contents as well as polyphenol oxidase (PPO) activity were assessed after camphor inhibition. Transcription and proteomics data from dormancy (D), sprouting (S), camphor inhibition (C), and recovery sprouting (R) samples showed changes in the expression levels of approximately 4000 transcripts, and 700 proteins showed different abundances. KEGG (Kyoto encyclopaedia of genes and genomes) pathway analysis of the transcription levels indicated that phytohormone synthesis and signal transduction play important roles in tuber sprouting. Camphor inhibited these processes, particularly for gibberellic acid, brassinosteroids, and ethylene, leading to dysregulation of physiological processes such as cutin, suberine and wax biosynthesis, fatty acid elongation, phenylpropanoid biosynthesis, and starch and sucrose metabolism, resulting in bud necrosis and prolonged storage periods. The KEGG pathway correlation between transcripts and proteins revealed that terpenoid backbone biosynthesis and plant–pathogen interaction pathways showed significant differences in D vs. S samples, but 13 pathways were remarkably different in the D vs. C groups, as camphor inhibition significantly increased both the transcription levels and protein abundance of pathogenesis-related protein PR-10a (or STH-2), the pathogenesis-related P2-like precursor protein, and the kirola-like protein as compared to sprouting. In recovery sprouting, these genes and proteins were decreased at both the transcriptional level and in protein abundance. It was important to find that the inhibitory effect of camphor on potato tuber sprout was reversible, revealing the action mechanism was similar to resistance to pathogen infection. The present study provides a theoretical basis for the application of camphor in prolonging seed potato storage.

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Section: Discussionmentioning

confidence: 99%

Comparative Morphology, Transcription, and Proteomics Study Revealing the Key Molecular Mechanism of Camphor on the Potato Tuber Sprouting Effect

Xue

Deng

et al. 2017

IJMS

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“…They identified seven proteins by using MALDI-TOF mass spectrometry, including cytochrome b6-f complex iron sulfur subunit, sHSP17.4, sHSP17.2, and sHSP26. Klein et al (2014) reported that sHSP17 and sHSP17.8 are molecular chaperones that protect maize cells from the effect of heat and other stresses. These results are in agreement with our results in which we used 2-DE technique and MALDI-TOF mass spectrometry to recognize and isolate the proteins involved in the response of the maize plant to HS treatment such as ATPase beta subunit, HSP/ Chaperonin, HSP 26, and HSP 16.9.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, the expression level of these five sHSPs can be considered as biomarkers for screening rice cultivars to avoid heat stress. Klein et al (2014) studied the expression and purification of two Class II sHSPs from Zea mays L. (cv. Oh43).…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis of heat shock proteins in maize (Zea mays L.)

et al. 2019

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Background: Maize is one of the important cereal food crops in the world. High temperature stress causes adverse influence on plant growth. When plants are exposed to high temperatures, they produce heat shock proteins (HSPs), which may impart a generalized role in tolerance to heat stress. Proteome analysis was performed in plant to assess the changes in protein types and their expression levels under abiotic stress. The purpose of the study is to explore which proteins are involved in the response of the maize plant to heat shock treatment. Results:We investigated the responses of abundant proteins of maize leaves, in an Egyptian inbred line of maize "K1", upon heat stress through two-dimensional electrophoresis (2-DE) on samples of maize leaf proteome. 2-DE technique was used to recognize heat-responsive protein spots using Coomassie Brilliant Blue (CBB) and silver staining. In 2-D analysis of proteins from plants treated at 45°C for 2 h, the results manifested 59 protein spots (4.3%) which were reproducibly detected as new spots where did not present in the control. In 2D for treated plants for 4 h, 104 protein spots (7.7%) were expressed only under heat stress. Quantification of spot intensities derived from heat treatment showed that twenty protein spots revealed clear differences between the control and the two heat treatments. Nine spots appeared with more intensity after heat treatments than the control, while four spots appeared only after heat treatments. Five spots were clearly induced after heat treatment either at 2 h or 4 h and were chosen for more analysis by LC-MSMS. They were identified as ATPase beta subunit, HSP26, HSP16.9, and unknown HSP/Chaperonin. Conclusion:The results revealed that the expressive level of the four heat shock proteins that were detected in this study plays important roles to avoid heat stress in maize plants.

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“…30 – 32 By forming stable complexes with folding or unfolding intermediate protein substrates, probably the molten globule, the sHSPs (which include alpha crystallin) can form large multimeric structures and have a wide range of cellular functions, including endowing cells with thermotolerance in vivo and being able to act as molecular chaperones in vitro. 33 , 34 Among them, HSPB1, HSPB4, and HSPB5 are responsible for the development of cataract, oncogenesis, and antiapoptotic activity. 35 – 37 The lens is largely formed from α-crystallin and βγ-crystallin superfamily with the main cellular partners of α-, β-, and γ-crystallin being abundant in vertebrate eye lens.…”

Section: Discussionmentioning

confidence: 99%

The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles

Li¹,

Han²,

Li³

et al. 2018

DDDT

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PurposeThe objective of this study was to investigate the effects of the solid lipid nanoparticles of baicalin (BA-SLNs) on an experimental cataract model and explore the molecular mechanism combined with bioinformatics analysis.Materials and methodsThe transparency of lens was observed daily by slit-lamp and photography. Lenticular opacity was graded. Two-dimensional gel electrophoresis (2-DE) was employed to analyze the differential protein expression modes in each group. Proteins of interest were subjected to protein identification by nano-liquid chromatography tandem mass spectrometry (LC–MS/MS). Bioinformatics analysis was performed using the Ingenuity Pathway Analysis (IPA) online software to comprehend the biological implications of the proteins identified by proteomics.ResultsAt the end of the sodium selenite-induced cataract progression, almost all lenses from the model group developed partial nuclear opacity; however, all lenses were clear and normal in the blank group. There was no significant difference between the BA-SLNs group and the blank group. Many protein spots were differently expressed in 2-DE patterns of total proteins of lenses from each group, and 65 highly different protein spots were selected to be identified between the BA-SLNs group and the model group. A total of 23 proteins were identified, and 12 of which were crystalline proteins.ConclusionWe considered crystalline proteins to play important roles in preserving the normal expression levels of proteins and the transparency of lenses. The general trend in the BA-SLN-treated lenses’ data showed that BA-SLNs regulated the protein expression mode of cataract lenses to normal lenses. Our findings suggest that BA-SLNs may be a potential therapeutic agent in treating cataract by regulating protein expression and may also be a strong candidate for future clinical research.

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Chaperone function of two small heat shock proteins from maize

Cited by 17 publications

References 69 publications

Comparative Morphology, Transcription, and Proteomics Study Revealing the Key Molecular Mechanism of Camphor on the Potato Tuber Sprouting Effect

Comparative Morphology, Transcription, and Proteomics Study Revealing the Key Molecular Mechanism of Camphor on the Potato Tuber Sprouting Effect

Proteomic analysis of heat shock proteins in maize (Zea mays L.)

The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles

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