Premium
Immunological evidence for a Physarum β‐tubulin polypeptide possessing an α‐tubulin‐like carboxyl terminus
Author(s) -
Gull Keith,
Wilcox Marianne,
Birkett Christopher R.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81185-7
Subject(s) - tubulin , physarum polycephalum , physarum , isotype , biology , microtubule , apicomplexa , biochemistry , microbiology and biotechnology , monoclonal antibody , antibody , genetics , plasmodium falciparum , immunology , malaria
A number of well‐characterised monoclonal antibodies have been produced which recognise either α‐ or β‐tubulin. One of these antibodies, YL1/2, has been regarded as a specific probe for α‐tubulin in that it recognises the linear amino acid sequence of the extreme C‐terminus of the α‐tubulin polypeptide. We now report that in the slime mould Physarum polycephalum , YL1/2 recognises the α‐tubulin isotype (α 1 ) that is expressed in the myxamoeba, but that it discriminates between the α 1 ‐tubulin sub‐types of the plasmodium ‐ the other major cell type in the Physarum life cycle; furthermore, YL1/2 does not recognise the plasmodium‐specific α‐tubulin isotype (α 1 ). Intriguingly, with plasmodial tubulin YL1/2 preferentially recognises a β‐tubulin, the plasmodium‐specific β 2 isotype. Reactivity with this one specific member of the β‐tubulin family is abolished by treatment of the tubulin with carboxypeptidase. Thus, the plasmodium‐specific β 2 ‐tubulin of Physarum appears to be a β‐tubulin with an α‐tubulin‐like carboxyl terminus.