Tubulin polyglycylation: a morphogenetic marker in ciliates.

Abstract:

:The occurrence of the tubulin post-translational modification, polyglycylation, in stable microtubular structures was investigated during morphogenesis in two ciliates, Paramecium and Frontonia atra, belonging to the Epiplasmata group. This analysis was carried out by means of immunofluorescence and post-embedding immunoelectron microscopy using two monoclonal antibodies, TAP 952 and AXO 49, respectively recognizing mono- and polyglycylated sites in alpha- and beta-tubulin. In the course of cell division, the TAP 952 epitope is detected in all microtubular structures including the newly assembled ones, such as cortical and oral basal bodies and cilia. In contrast, the AXO 49 epitope is only present in 'old' microtubular structures such as parental cortical and oral basal bodies and cilia. Our observations show that, in ciliates: 1) this tubulin post-translational modification takes place early in the course of morphogenesis; and 2) the lengthening of the polyglycine chains occurs after a great delay following addition of the first glycine residues on the tubulin glycylation sites, and following microtubule assembly. Thus, a sequential mechanism of polyglycylation is shown to take place in the tubulin molecule and during morphogenesis in Paramecium and Frontonia atra. Accordingly, polyglycylation, through a time-dependent polyglycine chain elongation process, appears to be a morphogenetic marker in ciliates.

journal_name

Biol Cell

journal_title

Biology of the cell

authors

Iftode F,Clérot JC,Levilliers N,Bré MH

doi

10.1016/s0248-4900(00)01107-2

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

615-28

issue

8-9

eissn

0248-4900

issn

1768-322X

journal_volume

92

pub_type

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