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β tubulin of bull sperm is polyglycylated
Author(s) -
Manfred Rüdiger,
Uwe Plessmann,
Rüdiger Ah,
Klaus Weber
Publication year - 1995
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(95)00373-h
Subject(s) - tubulin , sperm , microtubule , microbiology and biotechnology , paramecium , biology , chemistry , genetics
Car☐y‐terminal fragments of α and β tubulin from bull sperm were isolated and characterized by automated sequencing and mass spectrometry. About 60% of sperm α tubulin is polyglycylated. The lateral chain, which can reach 13 residues in length, is covalently attached via an isopeptide bond. The fully detyrosinated sperm α tubulin lacks polyglycylation. Thus mammalian sperm microtubules differ from the ciliary axonemal microtubules of the protozoan Paramecium for which others have documented a complete polyglycylation of both α and β tubulin.