Professor Yigongshi and Professor Jiawei Wang's group published article in Nature

In Spring of 2011，Professor Yigongshi and Professor Jiawei Wnag's group published an article titled as “ Structure and Mechanism of the Hexameric MecA–ClpC Molecular Machine” in the March 17 issue of the journal Nature, with the responding address as Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University.

As part of the post-translational quality control, ATP-dependent regulated proteolysis plays an indispensible role in all living cells: promptly removing unwanted proteins and regulatory proteins. In Bacteria, utilizing energy from the ATP hydrolysis, the members of Clp/Hsp100 family recognize, unfold and translocate proteins to the associated protease ClpP for degradation. In the Clp/Hsp100 family, ClpC with two NBDs domains is quite unique, the hexamerization and activation of ClpC requires an adaptor protein MecA. However the atomic details of the mechanism of ClpC activation and hexamerization by MecA still remains unknown.

In the June of 2007, Professor Shi and his group launched the project on the regulation mechanism of prokaryotic proteasome. After three years’ devoting work, the group solved three related crystal structures of MecA-ClpC in Bacillus Subtilis for the first time. In conjunction with biochemical analysis, their study demonstrates how MecA controls the assembly and activation of the ClpC hexamer, reveals the organizational principles of the hexameric Clp/Hsp100 proteins, resolves the controversy about the hexameric models of ClpB and Hsp104, and suggests how the MecA–ClpC molecular machine may recognize and unfold substrate proteins. This work is the landmark in the field of protein degradation machines, and provides the basis for studying the more complicated ubiquitin-26S proteasome in eukaryote technically and methodologically.

Notably, the two first authors of this article, Feng Wang and Ziqing Mei, were both post-doctoral researchers of School of Life Sciences. This article is the very first Nature article published by post-doctoral researchers from the school.