| Autor: |
Dibbayawan, Teresa P., Harper, John D.I., Elliott, Janet E., Gunning, Brian E.S., Marc, Jan |
| Zdroj: |
Cell Biology International; July 1995, Vol. 19 Issue: 7 p559-568, 10p |
| Abstrakt: |
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 Mr 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. Copyright 1995, 1999 Academic Press |
| Databáze: |
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