Plant Transglutaminases: New Insights in Biochemistry, Genetics, and Physiology

Cells. 2022 May 3;11(9):1529. doi: 10.3390/cells11091529.

Abstract

Transglutaminases (TGases) are calcium-dependent enzymes that catalyse an acyl-transfer reaction between primary amino groups and protein-bound Gln residues. They are widely distributed in nature, being found in vertebrates, invertebrates, microorganisms, and plants. TGases and their functionality have been less studied in plants than humans and animals. TGases are distributed in all plant organs, such as leaves, tubers, roots, flowers, buds, pollen, and various cell compartments, including chloroplasts, the cytoplasm, and the cell wall. Recent molecular, physiological, and biochemical evidence pointing to the role of TGases in plant biology and the mechanisms in which they are involved allows us to consider their role in processes such as photosynthesis, plant fertilisation, responses to biotic and abiotic stresses, and leaf senescence. In the present paper, an in-depth description of the biochemical characteristics and a bioinformatics comparison of plant TGases is provided. We also present the phylogenetic relationship, gene structure, and sequence alignment of TGase proteins in various plant species, not described elsewhere. Currently, our knowledge of these proteins in plants is still insufficient. Further research with the aim of identifying and describing the regulatory components of these enzymes and the processes regulated by them is needed.

Keywords: biochemical features; bioinformatics; physiological roles; plant transglutaminase.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Wall / metabolism
  • Chloroplasts / genetics
  • Chloroplasts / metabolism
  • Phylogeny
  • Plants* / genetics
  • Plants* / metabolism
  • Transglutaminases* / metabolism

Substances

  • Transglutaminases

Grants and funding

This work was supported by funds from the Poland–Italy Bilateral exchange programme Canaletto project: PO19MO03.