Purification, cloning and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa

An aspartic acid protease from common bean is expressed ‘on call’ during water stress and early recovery

“…These are stabilized by disulfur bridges hence forming heterodimers (Simões and Faro, 2004). In vitro studies have shown that this processing occurs mainly by autocleavage following a lowering of the pH Glathe et al, 1998;Asakura et al, 2000;Domingos et al, 2000;Castanheira et al, 2005). Based on our present protein gel blotting analysis together with previous data on AP-specific activity under drought stress in the same common bean cultivars (Cruz de Carvalho et al, 2001), we suggest that drought induced the processing/activation of PvAP1.…”

“…This group also includes a phytepsin from Centaura calciprata proposed to be involved in flower senescence (Domingos et al, 2000). Finally, group II assembles the phytepsins that have been related to biotic stress responses.…”

Two types of aspartic proteinases from buckwheat seed – Gene structure and expression analysis

“…In barley lectin, C-terminal peptide VFAEAIA was sufficient for the vacuolar targeting of the protein. Similar Cterminal motif VGFAEAA, found in FeAP9 as well as in some other plant APs, may also represent another vacuolar-targeting signal (Domingos et al, 2000), likely appropriate for specific types of vacuoles.…”

An unusual thermostable aspartic protease from the latex of Ficus racemosa (L.)

“…A BLAST search of the determined sequence did not show any matches with other plant proteases. Therefore the first 12 amino acid residues of the protease from F. racemosa were aligned and compared with amino-terminus sequences of other plant aspartic proteases (Table 4) and Leu corresponding to Val 7 and Leu 9 are the first conserved amino acids in plant aspartic proteases (Domingos et al, 2000). Leu 11 of F. racemosa protease corresponding to Leu 9 of phytepsin is conserved.…”