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

Walden, P; Blindt, AB; Birkett, C; Cox, R; Gull, K

Journal article

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

Abstract:: 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 6-11B-1, acetylated alpha-tubulin was detected in myxamoebae but not plasmodia of Physarum polycephalum. Following chemical acetylation plasmodial alpha-tubulin was detected by 6-11B-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 6-11B-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.

Publication status:: Published

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APA Style

Walden, P., Blindt, A. B., Birkett, C., Cox, R., & Gull, K. (1989). Recognition of specific Physarum alpha-tubulin isotypes by a monoclonal antibody. Sequence heterogeneity around the acetylation site at lysine 40. European Journal of Biochemistry / FEBS, 185(2), 383–389.

MLA Style

Walden, P., et al. “Recognition of Specific Physarum Alpha-Tubulin Isotypes by a Monoclonal Antibody. Sequence Heterogeneity around the Acetylation Site at Lysine 40.” European Journal of Biochemistry / FEBS, vol. 185, no. 2, 1989, pp. 383–89.

Chicago Style

Walden, P, AB Blindt, C Birkett, R Cox, and K Gull. 1989. “Recognition of Specific Physarum Alpha-Tubulin Isotypes by a Monoclonal Antibody. Sequence Heterogeneity around the Acetylation Site at Lysine 40.” European Journal of Biochemistry / FEBS 185 (2): 383–89.
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