POLYGLYCYLATION OF TUBULIN - A POSTTRANSLATIONAL MODIFICATION IN AXONEMAL MICROTUBULES

被引:233
作者
REDEKER, V
LEVILLIERS, N
SCHMITTER, JM
LECAER, JP
ROSSIER, J
ADOUTTE, A
BRE, MH
机构
[1] INST ALFRED FESSARD,CNRS,UNITE PROPRE RECH 2212,F-91198 GIF SUR YVETTE,FRANCE
[2] UNIV PARIS 11,BIOL CELLULAIRE LAB 4,CNRS,URA 1134,F-91405 ORSAY,FRANCE
[3] ECOLE POLYTECH,BIOCHIM LAB,CNRS,URA 240,F-91128 PALAISEAU,FRANCE
关键词
D O I
10.1126/science.7992051
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
A posttranslational modification was detected in the carboxyl-terminal region of axonemal tubulin from Paramecium. Tubulin carboxyl-terminal peptides were isolated and analyzed by Edman degradation sequencing, mass spectrometry, and amino acid analysis. All of the peptides, derived from both alpha and beta tubulin subunits, were modified by polyglycylation, containing up to 34 glycyl units covalently bound to the gamma carboxyl group of glutamyl residues. This modification, present in one of the most stable microtubular systems, may influence microtubule stability or axoneme function, or both.
引用
收藏
页码:1688 / 1691
页数:4
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