Plant Protein Biochemistry and Biomolecular Interactions

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Cell Biology".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 1451

Special Issue Editors


E-Mail Website
Guest Editor
1. Department of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK
2. School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK
Interests: cell biology; protein biochemistry; biomolecular interactions

E-Mail Website
Guest Editor
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA
Interests: cell wall polysaccharide biosynthesis; protein–protein interactions and structures; cell wall-mediated stress responses
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
Key Laboratory of State Forestry and Grassland Administration on Subtropical Forest Biodiversity Conservation, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China
Interests: alternative splicing in plants; functional proteomics; stress response; resource utilization of economic tree species
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Proteins carry out a wide variety of functions in plant growth and development as well as the stress response. By interacting with various partners such as DNA, RNA, ions, carbohydrates, lipids and other proteins, they can participate in transcription/translation regulation, signal transduction and metabolic catalysis, and provide structural support to cells. Biochemical and biophysics analysis is crucial for understanding how proteins function in biological processes. Structural approaches with X-ray crystallography have contributed mostly to our knowledge of protein function–structure associations; cryo-electron microscopy has revealed the molecular basis of protein complexes that comprise multiple components; and NMR has been used to probe interactions and conformational dynamics of proteins in solution, especially for investigating protein disorders.

Intrinsically disordered proteins (IDPs) challenge the classical structure–function paradigm with their disorder-to-order transition adopting various conformations via interacting with partners. Biomolecular condensates formed by liquid–liquid phase separation of IDPs serve as regulatory hubs to switch signaling and programming in cells. Thus, plant protein biochemistry must be revisited to understand the molecular mechanisms of how plant proteins are involved in various biological processes. This Special Issue will cover a wide variety of plant protein biochemistry areas to contribute to the overall knowledge of biomolecular interactions in plants and to call for novel tools and methods of protein biochemistry to study relevant processes and mechanisms.

Research articles, review articles and short communications are invited for submission.

Dr. An-Shan Hsiao
Prof. Dr. Olga A. Zabotina
Prof. Dr. Fuyuan Zhu
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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Plants is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein structure and function
  • protein–protein interactions
  • protein–RNA interactions
  • protein–lipid interactions
  • intrinsically disordered proteins
  • liquid–liquid phase separation
  • biomolecular condensates

Published Papers (2 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

14 pages, 6180 KiB  
Article
Plastid Molecular Chaperone HSP90C Interacts with the SecA1 Subunit of Sec Translocase for Thylakoid Protein Transport
by Adheip Monikantan Nair, Tim Jiang, Bona Mu and Rongmin Zhao
Plants 2024, 13(9), 1265; https://doi.org/10.3390/plants13091265 - 1 May 2024
Viewed by 686
Abstract
The plastid stroma-localized chaperone HSP90C plays a crucial role in maintaining optimal proteostasis within chloroplasts and participates in protein translocation processes. While existing studies have revealed HSP90C’s direct interaction with the Sec translocase-dependent client pre-protein PsbO1 and the SecY1 subunit of the thylakoid [...] Read more.
The plastid stroma-localized chaperone HSP90C plays a crucial role in maintaining optimal proteostasis within chloroplasts and participates in protein translocation processes. While existing studies have revealed HSP90C’s direct interaction with the Sec translocase-dependent client pre-protein PsbO1 and the SecY1 subunit of the thylakoid membrane-bound Sec1 translocase channel system, its direct involvement with the extrinsic homodimeric Sec translocase subunit, SecA1, remains elusive. Employing bimolecular fluorescence complementation (BiFC) assay and other in vitro analyses, we unraveled potential interactions between HSP90C and SecA1. Our investigation revealed dynamic interactions between HSP90C and SecA1 at the thylakoid membrane and stroma. The thylakoid membrane localization of this interaction was contingent upon active HSP90C ATPase activity, whereas their stromal interaction was associated with active SecA1 ATPase activity. Furthermore, we observed a direct interaction between these two proteins by analyzing their ATP hydrolysis activities, and their interaction likely impacts their respective functional cycles. Additionally, using PsbO1, a model Sec translocase client pre-protein, we studied the intricacies of HSP90C’s possible involvement in pre-protein translocation via the Sec1 system in chloroplasts. The results suggest a complex nature of the HSP90C-SecA1 interaction, possibly mediated by the Sec client protein. Our studies shed light on the nuanced aspects of HSP90C’s engagement in orchestrating pre-protein translocation, and we propose a potential collaborative role of HSP90C with SecA1 in actively facilitating pre-protein transport across the thylakoid membrane. Full article
(This article belongs to the Special Issue Plant Protein Biochemistry and Biomolecular Interactions)
Show Figures

Figure 1

19 pages, 3499 KiB  
Article
Interaction of Soybean (Glycine max (L.) Merr.) Class II ACBPs with MPK2 and SAPK2 Kinases: New Insights into the Regulatory Mechanisms of Plant ACBPs
by Atieh Moradi, Shiu-Cheung Lung and Mee-Len Chye
Plants 2024, 13(8), 1146; https://doi.org/10.3390/plants13081146 - 19 Apr 2024
Viewed by 543
Abstract
Plant acyl-CoA-binding proteins (ACBPs) function in plant development and stress responses, with some ACBPs interacting with protein partners. This study tested the interaction between two Class II GmACBPs (Glycine max ACBPs) and seven kinases, using yeast two-hybrid (Y2H) assays and bimolecular fluorescence [...] Read more.
Plant acyl-CoA-binding proteins (ACBPs) function in plant development and stress responses, with some ACBPs interacting with protein partners. This study tested the interaction between two Class II GmACBPs (Glycine max ACBPs) and seven kinases, using yeast two-hybrid (Y2H) assays and bimolecular fluorescence complementation (BiFC). The results revealed that both GmACBP3.1 and GmACBP4.1 interact with two soybean kinases, a mitogen-activated protein kinase MPK2, and a serine/threonine-protein kinase SAPK2, highlighting the significance of the ankyrin-repeat (ANK) domain in facilitating protein–protein interactions. Moreover, an in vitro kinase assay and subsequent Phos-tag SDS-PAGE determined that GmMPK2 and GmSAPK2 possess the ability to phosphorylate Class II GmACBPs. Additionally, the kinase-specific phosphosites for Class II GmACBPs were predicted using databases. The HDOCK server was also utilized to predict the binding models of Class II GmACBPs with these two kinases, and the results indicated that the affected residues were located in the ANK region of Class II GmACBPs in both docking models, aligning with the findings of the Y2H and BiFC experiments. This is the first report describing the interaction between Class II GmACBPs and kinases, suggesting that Class II GmACBPs have potential as phospho-proteins that impact signaling pathways. Full article
(This article belongs to the Special Issue Plant Protein Biochemistry and Biomolecular Interactions)
Show Figures

Figure 1

Back to TopTop