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PMID:2016300
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| Citation |
Evensen, G, Mathiesen, A and Sundan, A (1991) Direct molecular cloning and expression of two distinct abrin A-chains. J. Biol. Chem. 266:6848-52 |
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| Abstract |
The protein toxin abrin, which possesses an N-glycosylase activity toward eukaryotic 28 S rRNA, may have a potential in the deliberate eradication of certain cells. Here we report, by polymerase chain reaction technique, the isolation of genomic DNA sequences encoding two distinct abrin A-chains. A third sequence which encoded a part of a third type of A-chain was also isolated. The deduced amino acid sequences of the two full-length A-chains were about 84% similar. Addition of mRNA encoding the full-length A-chains to reticulocyte lysate strongly inhibited protein synthesis in the lysates, and a corresponding glycosylase activity on rRNA was observed. Addition of the same mRNA to toxin-resistant wheat germ extracts led to synthesis of the expected 30-kDa protein which could be precipitated with antibodies specific for abrin. |
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| Keywords |
Abrin/genetics; Amino Acid Sequence; Base Sequence; Cloning, Molecular; Gene Expression; Genetic Variation; Macromolecular Substances; Molecular Sequence Data; Oligonucleotide Probes; Polymerase Chain Reaction; RNA, Messenger/genetics; Restriction Mapping |
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