Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins, unrelated in amino-acid sequence, from Petrocoptis species.
Two new N-glycosidase type-1 ribosome-inactivating proteins (RIPs), denoted petroglaucin 1 and petrograndin, respectively, were isolated from the plants Petrocoptis glaucifolia (Lag.) Boiss sp. viscosa (Rothm.) Lainz and Petrocoptis grandiflora Rothm. These new RIPs do not share H2N-terminal amino-acid sequence homology with petroglaucin (now denoted as petroglaucin 2), the only other type-1 RIP to be isolated from P. glaucifolia (Arias et al. (1992) Planta 186, 532-540). Petroglaucin 1 shares amino-acid sequence homology with RIPs from Cucurbitaceae while petroglaucin 2 and petrograndin do so with saporins and dianthin 30 (Caryophyllaceae). The new RIPs strongly inhibited protein synthesis at subnanomolar concentrations in rabbit reticulocyte lysates and other eukaryotic cell-free systems, but they were inactive on bacterial ribosomes.
Arias
F J
FJ
Departamento de Bioquímica, Biología Molecular y Fisiología, Facultad de Ciencias, Universidad de Valladolid, Spain.
Rojo
M A
MA
Ferreras
J M
JM
Iglesias
R
R
Muñoz
R
R
Soriano
F
F
Méndez
E
E
Barbieri
L
L
Girbés
T
T
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000494:pharmacology; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D010940:Plant Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D010944:Plants / Q000737:chemistry*; D014176:Protein Biosynthesis / Q000187:drug effects; D012313:RNA / Q000187:drug effects; D012270:Ribosomes / Q000187:drug effects*; D017386:Sequence Homology, Amino Acid
D010940:Plant Proteins; D012313:RNA; D006026:Glycoside Hydrolases; D009699:N-Glycosyl Hydrolases; C091231:petroglaucin 1 protein, Petrocoptis glaucifolia; C091232:petrograndin