Characterization of the microtubule proteome during post-diapause development of Artemia franciscana

Biochimica Et Biophysica Acta
Paul A O'ConnellThomas H MacRae

Abstract

The microtubule proteome encompasses tubulin and a diverse group of proteins which associate with tubulin upon microtubule formation. These proteins either determine microtubule organization and function or their activity is influenced by microtubule association. To characterize the microtubule proteome in Artemia franciscana, tubulin assembly was induced with taxol in vitro after 0 and 12 h of post-diapause development. Proteins obtained by extraction of microtubules with 0.5 M NaCl were electrophoresed in two-dimensional gels and analyzed by mass spectrometry. Fifty-five proteins were identified with 10 of these occurring at both developmental stages, and multiple isoforms were observed for some proteins of the Artemia proteome. Their functions include roles in membrane transport, metabolism, chaperoning and protein synthesis, thus reflecting physiological properties of encysted Artemia such as stress resistance and the ability to rapidly initiate post-diapause development. For example, chaperones may protect tubulin during encystment and facilitate folding in metabolically active embryos. Additionally, the interaction of metabolic enzymes with microtubules funnels reaction intermediates, potentially enhancing efficiency with...Continue Reading

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Citations

Feb 20, 2008·Marine Biotechnology·Qian ZhouJianhai Xiang
May 25, 2007·Proceedings of the National Academy of Sciences of the United States of America·Joseph P RinehartDavid L Denlinger
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Mar 10, 2010·Cellular and Molecular Life Sciences : CMLS·Thomas H MacRae

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