Catalase and antiquitin from Euphorbia characias: two proteins involved in plant defense?
Here we report the cDNA nucleotide sequences of a calmodulin-binding catalase and an antiquitin from the latex of the Mediterranean shrub Euphorbia characias. Present findings suggest that catalase and antiquitin might represent additional nodes in the Euphorbia defense systems, and a multi-enzymatic interaction contributing to plant's protection against biotic and abiotic stresses is proposed to occur in E. characias laticifers.
Mura
A
A
Department of Applied Sciences in Biosystems, University of Cagliari, Monserrato (Cagliari), I-09042, Italy.
Pintus
F
F
Medda
R
R
Floris
G
G
Rinaldi
A C
AC
Padiglia
A
A
D000444:Aldehyde Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D002374:Catalase / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D028481:Euphorbia / Q000201:enzymology / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D007840:Latex / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism; D011485:Protein Binding; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017422:Sequence Analysis, DNA
D018076:DNA, Complementary; D007840:Latex; D010940:Plant Proteins; D002374:Catalase; D000444:Aldehyde Dehydrogenase