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Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly

The principal alpha-tubulin within Chlamydomonas reinhardtii flagellar axonemes differs from the major alpha-tubulin in the cell body. We show that these two isoelectric variants of alpha-tubulin are related to one another since posttranslational modification of the cell body precursor form converts...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112491/
https://www.ncbi.nlm.nih.gov/pubmed/6863393
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collection PubMed
description The principal alpha-tubulin within Chlamydomonas reinhardtii flagellar axonemes differs from the major alpha-tubulin in the cell body. We show that these two isoelectric variants of alpha-tubulin are related to one another since posttranslational modification of the cell body precursor form converts it to the axonemal form. During flagellar assembly, precursor alpha-tubulin enters the flagella and is posttranslationally modified within the flagellar matrix fraction prior to or at the time of its addition to the growing axonemal microtubules. Experiments designed to identify the nature of this posttranslational modification have also been conducted. When flagella are induced to assemble in the absence of de novo protein synthesis, tritiated acetate can be used to posttranslationally label alpha-tubulin in vivo and, under these conditions, no other flagellar polypeptides exhibit detectable labeling.
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spelling pubmed-21124912008-05-01 Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly J Cell Biol Articles The principal alpha-tubulin within Chlamydomonas reinhardtii flagellar axonemes differs from the major alpha-tubulin in the cell body. We show that these two isoelectric variants of alpha-tubulin are related to one another since posttranslational modification of the cell body precursor form converts it to the axonemal form. During flagellar assembly, precursor alpha-tubulin enters the flagella and is posttranslationally modified within the flagellar matrix fraction prior to or at the time of its addition to the growing axonemal microtubules. Experiments designed to identify the nature of this posttranslational modification have also been conducted. When flagella are induced to assemble in the absence of de novo protein synthesis, tritiated acetate can be used to posttranslationally label alpha-tubulin in vivo and, under these conditions, no other flagellar polypeptides exhibit detectable labeling. The Rockefeller University Press 1983-07-01 /pmc/articles/PMC2112491/ /pubmed/6863393 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
title Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
title_full Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
title_fullStr Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
title_full_unstemmed Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
title_short Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
title_sort chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112491/
https://www.ncbi.nlm.nih.gov/pubmed/6863393