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Recognition of specific Physarum -tubulin isotypes by a monoclonal antibody. Sequence heterogeneity around the acetylation site at lysine 40


Recognition of specific Physarum -tubulin isotypes by a monoclonal antibody. Sequence heterogeneity around the acetylation site at lysine 40



European Journal of Biochemistry 1852: 383-389



ISSN/ISBN: 0014-2956

DOI: 10.1111/j.1432-1033.1989.tb15126.x

The monoclonal antibody 6-11B-1 recognises specifically the acetylated form of .alpha.-tubulin. The acetylation event occurs on a unique lysine residue, lysine 40. Using 6-11 B-1, acetylated .alpha.-tubulin was detected in myxamoebae but not plasmodia of Physorum polycephalum. Following chemical acetylation plasmodial .alpha.-tubulin was detected by 6-11 B-1. The monoclonal antibody KMP-1 recognises certain Physarum .alpha.-tubulin isotypes but only in non-acetylated form. Whilst recognising all the non-acetylated fraction of myxamoebal .alpha.-tubulin only a proportion of plasmodial .alpha.-tubulin was recognised by KMP-1. Peptides were synthesised corresponding to the acetylation domains (containing lysine 40) of myxamoebal .alpha.-tubulin and the inferred acetylation domains of two plasmodial-specific .alpha.-tubulin isotypes. The only difference between the two peptides was at a single residue corresponding to amino acid 44 in the polypeptide. Tyrosine was present in myxamoebal .alpha.-tubulin and glycine was present in the plasmodial specific peptides; the peptides are referred to as the Tyr44 and Gly44 peptides respectively. Both peptides in acetylated form blocked 6-11 B-1 reactivity towards acetylated myxamoebal .alpha.-tubulin. The Tyr44 but not the Gly44 peptide blocked KMP-1 reactivity towards non-acetylated myxamoebal .alpha.-tubulin. Tyrosine at position 44 is not found in any other known .alpha.-tubulin. Thus a unique antigenic determinant exists in certain Physarum .alpha.-tubulin isotypes, close to the acetylation site at lysine 40. This antigenic determinant forms part of the KMP-1 recognition epitope and explains the unique isotype selectivity of this monoclonal antibody.

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Accession: 021646696

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