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Báo cáo khoa học: Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonica A)

Lamjapin,anoveltypeIribosome-inactivating protein, has been isolated from kelp (Laminaria japonicaA), a marine alga. This protein has been extensively purified through multiple chromatography columns. With a molecular mass of 36 kDa, lamjapin is slightly larger than the other known single-chain ribosome-inactivating proteins from the higher plants. Lamjapin can inhibit protein synthesis in rabbit reticulocyte lysate with an IC50 of 0.69 nM. | Eur. J. Biochem. 269 4746-4752 2002 FEBS 2002 doi 10.1046 j.1432-1033.2002.03165.x Isolation and enzymatic characterization of lamjapin the first ribosome-inactivating protein from cryptogamic algal plant Laminaria japonica A Ren-shui Liu1 Jia-hua Yang2 and Wang-Yi Liu1 1 State Key Laboratory of Molecular Biology Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences China department of Biochemistry Yantai University Shandong China Lamjapin a novel type I ribosome-inactivating protein has been isolated from kelp Laminaria japonica A a marine alga. This protein has been extensively purified through multiple chromatography columns. With a molecular mass of w 36 kDa lamjapin is slightly larger than the other known single-chain ribosome-inactivating proteins from the higher plants. Lamjapin can inhibit protein synthesis in rabbit reticulocyte lysate with an IC50 of 0.69 nM. It can depurinate at multiple sites of RNA in rat ribosome and produce the diagnostic R-fragment and three additional larger fragments after the aniline reaction. Lamjapin can deadenylate specifically at the site A20 of the synthetic oligoribonucleotide 35-mer substrate that mimics the sarcin ricin domain SRD of rat ribosomal 28S RNA. However it cannot hydrolyze the N-C glycosidic bond of guanosine cytidine or uridine at the corresponding site of the A20 of three mutant SRD RNAs. Lamjapin exhibits the same base and position requirement as the ribosome-inactivating proteins from higher plants. We conclude that lamjapin is an RNA N-glycosidase that belongs to the ribosome-inactivating protein family. This study reports for the first time that ribosome-inactivating protein exists in the lower cryp-togamic algal plant. Keywords kelp lamjapin marine alga ribosome-inactivating protein RNA N-glycosidase. Plant ribosome-inactivating proteins RIPs are a group of toxic proteins with RNA N-glycosidase activity that act on the eukaryotic and .