Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila.

Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila.
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DOI:
10.1083/jcb.149.5.1097
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发表时间:
2000-05-29
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Gaertig J
Gaertig J
中科院分区:
其他
文献类型:
--
作者:
Xia L;Hai B;Gao Y;Burnette D;Thazhath R;Duan J;Bré MH;Levilliers N;Gorovsky MA;Gaertig J

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We analyzed the role of tubulin polyglycylation in Tetrahymena thermophila using in vivo mutagenesis and immunochemical analysis with modification-specific antibodies. Three and five polyglycylation sites were identified at glutamic acids near the COOH termini of α- and β-tubulin, respectively. Mutants lacking all polyglycylation sites on α-tubulin have normal phenotype, whereas similar sites on β-tubulin are essential. A viable mutant with three mutated sites in β-tubulin showed reduced tubulin glycylation, slow growth and motility, and defects in cytokinesis. Cells in which all five polyglycylation sites on β-tubulin were mutated were viable if they were cotransformed with an α-tubulin gene whose COOH terminus was replaced by the wild-type COOH terminus of β-tubulin. In this double mutant, β-tubulin lacked detectable polyglycylation, while the α-β tubulin chimera was hyperglycylated compared with α-tubulin in wild-type cells. Thus, the essential function of polyglycylation of the COOH terminus of β-tubulin can be transferred to α-tubulin, indicating it is the total amount of polyglycylation on both α- and β-tubulin that is essential for survival.
在嗜热四膜虫中,赖氨酸40在α-微管蛋白中的乙酰化并不是必需的。
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发表时间: 1995-06
影响因子: 7.8
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