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Structural/Functional Characterization of Plant Proteins 2.0
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Structural/Functional Characterization of Plant Proteins 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Plant Sciences".

Deadline for manuscript submissions: closed (30 September 2022) | Viewed by 9211

Special Issue Editors

Prof. Dr. Alessio Scarafoni

E-Mail Website
Guest Editor
Department of Food, Environmental and Nutritional Sciences, Università degli Studi di Milano, 20122 Milan, Italy
Interests: food recycling; plant enzyme inhibitors; protein structure and function; recombinant proteins; seed germination; seed storage proteins
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Stefania Iametti

E-Mail Website
Co-Guest Editor
Department of Food, Environmental and Nutritional Sciences, University of Milan, DISMA, Via G Celoria 2, I-20133 Milan, Italy
Interests: food allergens; structural investigation methodologies

Special Issue Information

Dear Colleagues,

Disentangling the relationship between protein structure and function continues to be a priority not only in several fields of structural biology, including molecular biology, biochemistry, and protein engineering, but also in plant physiology and food sciences, including new industrial applications.

It is a well-established fact that even minor structural variations in a protein may dramatically affect its function and its capacity to interact with other molecules, no matter which structural level is involved. Moreover, protein conformation is influenced, and can be modified, by its environmental surrounding. This is especially true for plant proteins that find applications in several complex systems.

Today, there is an increasing interest in plant proteins. In specialized reserve tissues, plants are able to accumulate huge amounts of proteins with unique and interesting structural features.

Apart from their natural biology, nutritional impact, and relevance to the food industry, plant proteins find applications in a variety of nonfood systems. These are usually complex systems where the interactions between different components are key factors that determine and influence some typical features of the final product.

This Special Issue aims to present the current status of knowledge on plant proteins, in the broadest context, and to contribute to their exploitation and valorization. We welcome research papers and reviews that expand knowledge about the molecular determinants driving their structure–function relationships, including in vivo and in vitro interactions with other proteins and other macromolecules as well as their potential for innovative applications in all fields, taking into account bioactivities implicated in human nutrition and health.

Prof. Stefania Iametti
Prof. Alessio Scarafoni
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Keywords

  • protein–protein interactions
  • protein structure
  • complex systems
  • food systems
  • plant biochemistry
  • plant seeds

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Published Papers (3 papers)

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Research

19 pages, 2831 KiB  
Article
β-Conglutins’ Unique Mobile Arm Is a Key Structural Domain Involved in Molecular Nutraceutical Properties of Narrow-Leafed Lupin (Lupinus angustifolius L.)
by Elena Lima-Cabello, Julia Escudero-Feliu, Andreina Peralta-Leal, Pedro Garcia-Fernandez, Kadambot H. M. Siddique, Karam B. Singh, Maria I. Núñez, Josefa León and Jose C. Jimenez-Lopez
Int. J. Mol. Sci. 2023, 24(8), 7676; https://doi.org/10.3390/ijms24087676 - 21 Apr 2023
Cited by 1 | Viewed by 2509
Abstract
Narrow-leafed lupin (NLL; Lupinus angustifolius L.) has multiple nutraceutical properties that may result from unique structural features of β-conglutin proteins, such as the mobile arm at the N-terminal, a structural domain rich in α-helices. A similar domain has not been found in other [...] Read more.
Narrow-leafed lupin (NLL; Lupinus angustifolius L.) has multiple nutraceutical properties that may result from unique structural features of β-conglutin proteins, such as the mobile arm at the N-terminal, a structural domain rich in α-helices. A similar domain has not been found in other vicilin proteins of legume species. We used affinity chromatography to purify recombinant complete and truncated (without the mobile arm domain, tβ5 and tβ7) forms of NLL β5 and β7 conglutin proteins. We then used biochemical and molecular biology techniques in ex vivo and in vitro systems to evaluate their anti-inflammatory activity and antioxidant capacity. The complete β5 and β7 conglutin proteins decreased pro-inflammatory mediator levels (e.g., nitric oxide), mRNA expression levels (iNOS, TNFα, IL-1β), and the protein levels of pro-inflammatory cytokine TNF-α, interleukins (IL-1β, IL-2, IL-6, IL-8, IL-12, IL-17, IL-27), and other mediators (INFγ, MOP, S-TNF-R1/-R2, and TWEAK), and exerted a regulatory oxidative balance effect in cells as demonstrated in glutathione, catalase, and superoxide dismutase assays. The truncated tβ5 and tβ7 conglutin proteins did not have these molecular effects. These results suggest that β5 and β7 conglutins have potential as functional food components due to their anti-inflammatory and oxidative cell state regulatory properties, and that the mobile arm of NLL β-conglutin proteins is a key domain in the development of nutraceutical properties, making NLL β5 and β7 excellent innovative candidates as functional foods. Full article
(This article belongs to the Special Issue Structural/Functional Characterization of Plant Proteins 2.0)
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15 pages, 2888 KiB  
Article
The DnaJ-like Zinc Finger Protein ORANGE Promotes Proline Biosynthesis in Drought-Stressed Arabidopsis Seedlings
by Farman Ali, Qi Wang, Aliya Fazal, Lin-Juan Wang, Shuyan Song, Meng-Juan Kong, Tariq Mahmood and Shan Lu
Int. J. Mol. Sci. 2022, 23(7), 3907; https://doi.org/10.3390/ijms23073907 - 31 Mar 2022
Cited by 14 | Viewed by 2505
Abstract
Orange (OR) is a DnaJ-like zinc finger protein with both nuclear and plastidial localizations. OR, and its orthologs, are highly conserved in flowering plants, sharing a characteristic C-terminal tandem 4× repeats of the CxxCxxxG signature. It was reported to trigger chromoplast biogenesis, promote [...] Read more.
Orange (OR) is a DnaJ-like zinc finger protein with both nuclear and plastidial localizations. OR, and its orthologs, are highly conserved in flowering plants, sharing a characteristic C-terminal tandem 4× repeats of the CxxCxxxG signature. It was reported to trigger chromoplast biogenesis, promote carotenoid accumulation in plastids of non-pigmented tissues, and repress chlorophyll biosynthesis and chloroplast biogenesis in the nucleus of de-etiolating cotyledons cells. Its ectopic overexpression was found to enhance plant resistance to abiotic stresses. Here, we report that the expression of OR in Arabidopsis thaliana was upregulated by drought treatment, and seedlings of the OR-overexpressing (OE) lines showed improved growth performance and survival rate under drought stress. Compared with the wild-type (WT) and OR-silencing (or) lines, drought-stressed OE seedlings possessed lower contents of reactive oxygen species (such as H2O2 and O2−), higher activities of both superoxide dismutase and catalase, and a higher level of proline content. Our enzymatic assay revealed a relatively higher activity of Δ1-pyrroline-5-carboxylate synthase (P5CS), a rate-limiting enzyme for proline biosynthesis, in drought-stressed OE seedlings, compared with the WT and or lines. We further demonstrated that the P5CS activity could be enhanced by supplementing exogenous OR in our in vitro assays. Taken together, our results indicated a novel contribution of OR to drought tolerance, through its impact on proline biosynthesis. Full article
(This article belongs to the Special Issue Structural/Functional Characterization of Plant Proteins 2.0)
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14 pages, 7131 KiB  
Article
Chromatography-Independent Fractionation and Newly Identified Molecular Features of the Adzuki Bean (Vigna angularis Willd.) β-vignin Protein
by Biane Philadelpho, Victória Souza, Fabiani Souza, Johnnie Santos, Fabiana Batista, Mariana Silva, Jessica Capraro, Stefano De Benedetti, Giuditta C. Heinzl, Eduardo Cilli, Alessio Scarafoni, Chiara Magni and Ederlan Ferreira
Int. J. Mol. Sci. 2021, 22(6), 3018; https://doi.org/10.3390/ijms22063018 - 16 Mar 2021
Cited by 6 | Viewed by 3084
Abstract
Adzuki seed β-vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure [...] Read more.
Adzuki seed β-vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure has been optimized and described. The electrophoretic analysis showed a high degree of homogeneity of β-vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean β-vignin was found to have a native size of 146 kDa, and the molecular weight determined was consistent with a trimeric structure. These were identified in two main polypeptide chains (masses of 56–54 kDa) that are glycosylated polypeptides with metal binding capacity, and one minor polypeptide chain with a mass 37 kDa, wherein these features are absent. The in vitro analysis showed a high degree of digestibility of the protein (92%) and potential anti-inflammatory capacity. The results lay the basis not only for further investigation of the health-promoting properties of the adzuki bean β-vignin protein, but also for a possible application as nutraceutical molecule. Full article
(This article belongs to the Special Issue Structural/Functional Characterization of Plant Proteins 2.0)
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