Application of Escherichia coli Chip in Studying Protein Deacetylase YcgC

Researchers at Shanghai Jiaotong University and Johns Hopkins University in the United States have discovered a new protein deacetylase YcgC using the E. coli proteome produced by Guangzhou Boao Biotechnology Co., Ltd., the research results 2015 12 Published online in eLIFE magazine on the 30th.
Protein is the embodiment of life activities, and it is often modified in different types during the life cycle. As an important and widespread type of post-translational modification of proteins, acetylation is closely related to a range of important diseases, affecting many key biological processes. With the advancement of proteomic technology, thousands of acetylation modifications have been found in cells of many organisms, from lower E. coli to higher humans. Acetylation of proteins is regulated by acetyltransferases and deacetylases. Corresponding to the massive protein acetylation modification, the number of known acetylases and deacetylases is very limited, and a considerable number of new enzymes remain to be discovered. A key question is "How to achieve the discovery of efficient acetylation-related enzymes?" .

In response to this problem, the researchers developed a technique called " Clip-chip ". Based on the E. coli proteome chip, a global protein deacetylase was studied and a new one was discovered. Deacetylase YcgC. This enzyme is very efficient in removing the acetylation of the substrate protein RutR lysine 52 and lysine 62. Known protein deacetylase activity is dependent on NAD + or Zn 2+, but YcgC deacetylation activity is not dependent on the above two. Further functional experiments indicate that YcgC affects the transcriptional regulatory activity of RutR by deacetylation. In the experiment, the researchers also found that RutR has protease activity, and YcgC can regulate the protease activity of RutR by deacetylation. The researchers compared the effect of YcgC and E. coli, the only deacetylase, on the expression profile of E. coli. The results showed that the two have similarities and large differences, suggesting the substrate spectrum of YcgC and the possibility of CobB. There is a big difference. Through whole-genome synthesis, the researchers obtained homologous gene clones of Escherichia coli YcgC derived from a number of other bacteria, and expression tests showed that the proteins expressed by these clones all had protein deacetylase activity.

The YcgC found in the study may represent a new family of protein deacetylases. At the same time, the Clip-Chip technology developed in this study is versatile and can be easily transplanted into the discovery of other enzymes.
The E. coli proteome used in this study has been transformed and produced by Guangzhou Boao Biotechnology Co., Ltd. , and it is hoped that more researchers will provide this group of research tools!
Original link: http://elifesciences.org/content/4/e05322

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