DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin.
DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin.
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DOI：
10.1016/j.str.2015.01.010
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发表时间：
2015-03-03
期刊：
影响因子：
5.7
通讯作者：
Fushman, David
中科院分区：
文献类型：
--
作者：
Nowicka, Urszula;Zhang, Daoning;Walker, Olivier;Krutauz, Daria;Castaneda, Carlos A.;Chaturvedi, Apurva;Chen, Tony Y.;Reis, Noa;Glickman, Michael H.;Fushman, David
Ddi1 belongs to a family of shuttle proteins targeting polyubiquitinated substrates for proteasomal degradation. Unlike the other proteasomal shuttles, Rad23 and Dsk2, Ddi1 remains an enigma: its function is not fully understood and structural properties are poorly characterized. We determined the structure and binding properties of the ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains of Ddi1 from Saccharomyces cerevisiae. We found that, while Ddi1UBA forms a characteristic UBA:ubiquitin complex, Ddi1UBL has entirely uncharacteristic binding preferences. Despite having a ubiquitin-like fold, Ddi1UBL does not interact with typical UBL-receptors but, unexpectedly, binds ubiquitin, forming a unique interface mediated by hydrophobic contacts and by salt-bridges between oppositely-charged residues of Ddi1UBL and ubiquitin. In stark contrast with ubiquitin and other UBLs, the β-sheet surface of Ddi1UBL is negatively charged and, therefore, is recognized in a completely different way. The dual functionality of Ddi1UBL, capable of binding both ubiquitin and proteasome, suggests a novel mechanism for Ddi1 as a proteasomal shuttle.
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影响因子：
5.6
作者：
Kang, Y;Vossler, RA;Walters, KJ
通讯作者：
Walters, KJ
影响因子：
5.3
作者：
Clarke, DJ;Mondesert, G;Reed, SI
通讯作者：
Reed, SI
DOI：
10.3410/b3-26
发表时间：
2011
期刊：
F1000 biology reports
影响因子：
--
作者：
Fushman D;Wilkinson KD
通讯作者：
Wilkinson KD
影响因子：
7.7
作者：
Chen, L;Shinde, U;Madura, K
通讯作者：
Madura, K
影响因子：
14.8
作者：
De Vries, Sjoerd J.;van Dijk, Marc;Bonvin, Alexandre M. J. J.
通讯作者：
Bonvin, Alexandre M. J. J.