Intra- and intersubunit changes accompanying thermal activation of the HtrA2(Omi) protease homotrimer
详细信息 查看全文
- 作者：Miroslaw Jarzaba ; 1 ; Tomasz Wentaa ; 1 ; Dorota Zurawa-Janickaa ; Agnieszka Politb ; Artur J. Gieldonc ; Magdalena Wysockac ; Przemyslaw Glazaa ; Joanna Skorko-Gloneka ; Jerzy Ciarkowskic ; Adam Lesnerc ; Barbara Lipinskaa ; barbara.lipinska@biol.ug.edu.pl" class="auth_mail" title="E-mail the corresponding author
- 关键词：PD ; protease domain ; PD* ; protease domain of the neighboring subunit ; PDZ domain ; domain with homology to postsynaptic density of 95 ; kDa ; disc large and zonula occludens 1 proteins ; Fw ; fluorescence intensity of a labeled protein with tryptophan residue ; F0 ; fluorescence intensity of a labeled protein without tryptophan residue ; τw ; fluorescence lifetime of a labeled protein with tryptophan residue ; τ0 ; fluorescence lifetime of a labeled protein without tryptophan residue ; mBBr ; monobromobi
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：1864
- 期：3
- 页码：283-296
- 全文大小：2534 K
文摘
- •
Upon activation, the HtrA2 PDZ domain changes its position versus protease domain.
- •
The change occurs inside a subunit and between the subunits of the HtrA2 trimer.
- •
The α5 helix of PDZ is involved in both, the intra- and intersubunit changes.
- •
The changes involve the L3 and L1 regulatory loops of the protease.
- •
The mutations decreasing the interdomain interactions promote HtrA2 activity.