The amino-acid sequence of two non-toxic mutants of diphtheria toxin: CRM45 and CRM197 - PubMed (original) (raw)

The amino-acid sequence of two non-toxic mutants of diphtheria toxin: CRM45 and CRM197

G Giannini et al. Nucleic Acids Res. 1984.

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Abstract

The amino-acid sequences of two diphtheria toxin-related, non-toxic proteins, CRM45 and CRM197 , were deduced from the complete sequence of their genes: tox 45 and tox 197. CRM45 lacks the last 149 C-terminal amino-acid residues, but is otherwise identical to diphtheria toxin: a single C----T transition introduces an "ochre" (TAA) termination signal in tox 45, after the codon for threonine-386. A single G----A transition was also found in tox 197, leading to the substitution of glycine-52, present in the wild-type toxin, with glutamic acid in CRM197 . This aminoacid change is responsible for the loss of the NAD:EF2 ADP-ribosyltransferase activity in CRM197 , due most probably to an alteration of the NAD+ binding site.

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References

    1. J Biol Chem. 1974 Apr 10;249(7):2088-97 - PubMed
    1. J Biol Chem. 1973 Jun 10;248(11):3851-4 - PubMed
    1. Biochim Biophys Acta. 1977 Mar 28;491(1):286-95 - PubMed
    1. Annu Rev Biochem. 1977;46:69-94 - PubMed
    1. J Bacteriol. 1978 Dec;136(3):1135-42 - PubMed

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