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- W2050993411 abstract "To obtain information on plant microtubule stability to low temperature and Ca2+, the regulatory domain of polymerized tubulin from maize (Zea mays ev. Black Mexican Sweet) was dissected by limited proteolysis with subtilisin. Tubulin in taxol-stabilized microtubules was cleaved in a subtilisin concentration- and time-dependent manner. Immunoblotting of microtubules with antibodies having mapped epitopes on α- and β-tubulins revealed that cleavage initially removed ≤15 residues from the β-tubulin carboxyl terminus to produce αβs-microtubules. Subsequent cleavage occurred at an extreme site and an internal site within the α-tubulin carboxyl terminus. Electron microscopy revealed that αβs-microtubules were ultra structurally indistinguishable from uncleaved control αβ-micro-tubules. Quantitative polymer sedimentation showed that low temperature treatment (0°C) caused significant depolymerization of αβ-microtubules, but little depolymerization of αβs-microtubules. Ca2+ enhanced the cold-induced depolymerization of both αβ- and αβs-microtubules. However, αβs-microtubules were significantly more stable to depolymerization by cold and Ca2+ than were αβ-micro-tubules. The results showed that maize microtubules containing shortened β-tubulin carboxyl termini are relatively resistant to the combined depolymerizing effects of cold and Ca2+. Thus, the extreme carboxyl terminus of β-tubulin is a crucial element of the plant tubulin regulatory domain and may be involved in the modulation of microtubule stability during the chilling response in plants." @default.
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- W2050993411 date "1996-05-01" @default.
- W2050993411 modified "2023-09-27" @default.
- W2050993411 title "Proteolytic analysis of polymerized maize tubulin: regulation of microtubule stability to low temperature and Ca2+ by the carboxyl terminus of beta-tubulin" @default.
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- W2050993411 doi "https://doi.org/10.1111/j.1365-3040.1996.tb00387.x" @default.
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