A γ-tubulin that associates specifically with centrioles in HeLa cells and the basal body complex in Chlamydomonas
✍ Scribed by Teresa P. Dibbayawan; John D.I. Harper; Janet E. Elliott; Brian E.S. Gunning; Jan Marc
- Book ID
- 102966164
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 866 KB
- Volume
- 19
- Category
- Article
- ISSN
- 1065-6995
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✦ Synopsis
Abstract
γ‐Tubulin is a putative component of microtubule initiating material. To further explore its subcellular distribution in plant and animal cells, we have raised a polyclonal antibody, Rb27, directed towards a conserved region (EEFATEGTDRKDVFFY) of the γ‐tubulin molecule. Immunoblotting of cell protein extracts with Rb27 reveals a polypeptide band of M~r~ 49 kD in HeLa and a 58 kD band in Chlamydomonas. Although these polypeptides are comparable in size to forms of γ‐tubulin detected previously in mammalian and plant protein extracts by other antibodies to γ‐tubulin, by immunofluorescence microscopy Rb27 gives localization patterns not previously seen. It localizes specifically with the centrioles in HeLa cells and with the basal body complex in Chlamydomonas. Other γ‐tubulin antibodies label pericentriolar material. Because of the similarities in the size of the polypeptides recognized by our and other γ‐tubulin antibodies, and a restricted co‐localization with known microtubule‐organizing centres in evolutionarily distant organisms, we propose that Rb27 recognizes a novel conserved γ‐tubulin isotype.