Proteases and Protease Inhibitors in Plant Growth, Development, Stress Responses and Plant Biotechnological Applications

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

Deadline for manuscript submissions: closed (30 April 2022) | Viewed by 4318

Special Issue Editor


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Guest Editor
Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada
Interests: somatic embryogenesis; conifer biotechnology; matrix metalloproteinases; endophyte–plant interactions; tissue culture

Special Issue Information

Dear Colleagues,

Proteolysis is involved in various aspects of plant development, stress responses and overall physiology. These aspects include signal molecule generation via precursor protein processing, general protein turnover, senescence, defense against pathogens and pests, seed storage protein mobilization, and nutrient acquisition by carnivorous plants. The regulation of protease activity, whether at the level of the individual proteases themselves or the regulation of specific protease inhibitor classes, is of significance if we are to understand the overall importance of proteolytic activity in plant biology, as well as the potential biotechnological applications of regulated proteolytic activity.

In addition to intracellular localization, numerous proteomic studies have indicated that various proteases and protease inhibitors are secreted into the extracellular matrix environment. The regulation and role of protease activity require further characterization and key questions remain to be answered. How is overall proteolytic activity controlled in the plant extracellular matrix? What molecular mechanisms regulate these proteases and protease inhibitors? How are inactive precursors processed to generate active proteases? What are the extracellular substrates of these proteases? How do these proteases and their respective inhibitors impact plant growth, development and stress responses? How can proteases and protease inhibitors be used in biotechnological applications?

This Special Issue of Plants is aimed at addressing these questions. It focuses on secreted, proteases and protease inhibitors and seeks to compile novel results in this field of research as well as literature reviews of subjects related to this field.

Dr. Barry Flinn
Guest Editor

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Keywords

  • protease
  • protease inhibitor
  • proteolysis
  • extracellular matrix
  • apoplast

Published Papers (1 paper)

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Review

29 pages, 3045 KiB  
Review
Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications
by Anis Baharin, Tiew-Yik Ting and Hoe-Han Goh
Plants 2022, 11(10), 1330; https://doi.org/10.3390/plants11101330 - 18 May 2022
Cited by 7 | Viewed by 3793
Abstract
Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are several [...] Read more.
Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are several classes of proteases in the MEROPS database based on their catalytic mechanisms. This review focuses on post-proline cleaving enzymes (PPCEs) from different peptidase families, as well as prolyl endoprotease/oligopeptidase (PEP/POP) from the serine peptidase family. To date, most PPCEs studied are of microbial and animal origins. Recently, there have been reports of plant PPCEs. The most common PEP/POP are members of the S9 family that comprise two conserved domains. The substrate-limiting β-propeller domain prevents unwanted digestion, while the α/β hydrolase catalyzes the reaction at the carboxyl-terminal of proline residues. PPCEs display preferences towards the Pro-X bonds for hydrolysis. This level of selectivity is substantial and has benefited the brewing industry, therapeutics for celiac disease by targeting proline-rich substrates, drug targets for human diseases, and proteomics analysis. Protein engineering via mutagenesis has been performed to improve heat resistance, pepsin-resistant capability, specificity, and protein turnover of PPCEs for pharmacological applications. This review aims to synthesize recent structure–function studies of PPCEs from different families of peptidases to provide insights into the molecular mechanism of prolyl cleaving activity. Despite the non-exhaustive list of PPCEs, this is the first comprehensive review to cover the biochemical properties, biological functions, and biotechnological applications of PPCEs from the diverse taxa. Full article
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