Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme

被引:25
作者
Kakhniashvili, DG
Chaudhary, T
Zimmer, WE
Bencsath, FA
Jardine, I
Goodman, SR [1 ]
机构
[1] Univ S Alabama, Coll Med, Dept Neurosci & Cell Biol, Mobile, AL 36688 USA
[2] Univ S Alabama, Coll Med, Dept Biochem & Mol Biol, Mobile, AL 36688 USA
[3] Univ S Alabama, Coll Med, Ctr Comprehens Sickle Cell, Mobile, AL 36688 USA
[4] Thermoquest, San Jose, CA 95134 USA
[5] US FDA, Gulf Coast Seafood Lab, Dauphin Isl, AL 36528 USA
关键词
D O I
10.1021/bi010176t
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The involvement of red blood cell spectrin in the ubiquitination process was studied. Spectrin was found to form two ubiquitin-associated derivatives, a DTT-sensitive ubiquitin adduct and a DTT-insensitive conjugate, characteristic intermediate and final products of the ubiquitination reaction cascade. In addition to spectrin and ubiquitin, ubiquitin-activating enzyme (El) and ATP were necessary and sufficient to form both the spectrin-ubiquitin adduct and conjugate. No exogenous ubiquitin-conjugating (E2) or ligase (E3) activities were required, suggesting that erythrocyte spectrin is an E2 ubiquitin-conjugating enzyme able to target itself. Both ubiquitin adduct and conjugate were linked to the alpha subunit of spectrin, suggesting that the ubiquitin-conjugating (UBC) domain and its target regions reside on the same subunit.
引用
收藏
页码:11630 / 11642
页数:13
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