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Plant type I metacaspases are proteolytically active proteases despite their hydrophobic nature
Author(s) -
van Midden Katarina Petra,
Peric Tanja,
Klemenčič Marina
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14165
Subject(s) - proteases , serpin , cysteine , chemistry , biochemistry , proteolysis , cysteine protease , caspase , cleavage (geology) , microbiology and biotechnology , biology , enzyme , programmed cell death , apoptosis , gene , paleontology , fracture (geology)
Plant metacaspases type I (MCA‐Is), the closest structural homologs of caspases, are key proteases in stress‐induced regulated cell death processes in plants. However, no plant MCA‐Is have been characterized in vitro to date. Here, we show that only plant MCA‐Is contain a highly hydrophobic loop within the C terminus of their p10 domain. When removed, soluble and proteolytically active plant MCA‐Is can be designed and recombinantly produced. We show that the activity of MCA‐I depends on calcium ions and that removal of the hydrophobic loop does not affect cleavage and covalent binding to its inhibitor SERPIN. This novel approach will finally allow the development of tools to detect and manipulate the activity of these cysteine proteases in vivo and in planta .