In:
eLife, eLife Sciences Publications, Ltd, Vol. 4 ( 2015-12-30)
Abstract:
After proteins have been made, they can be modified in several ways. For example, chemical tags called acetyl groups may be added to (and later removed from) the protein to regulate cell activities such as aging and metabolism. Enzymes are proteins that help catalyze the reactions that add or remove the acetyl tags on certain “substrate” proteins. In the bacteria species Escherichia coli, many enzymes that help to add acetyl groups to proteins have been discovered. However, only a single E. coli “deacetylase” enzyme that removes the acetyl group has been identified. Now, Tu, Guo, Chen et al. have devised a technique to identify new deacetylases, called the “clip-chip” approach. In this method, thousands of proteins that are potential deacetylases are arrayed on a glass slide, and substrate proteins are immobilized on another slide. The two slides are then clipped together face-to-face, allowing the potential enzymes to transfer to the substrate slide and interact with the substrates. Using this approach, Tu, Guo, Chen et al. identified a protein called YcgC as a deacetylase in bacteria. Further characterization experiments revealed that YcgC works in a different way to other known deacetylases, and that it targets different substrates to the previously known E. coli deacetylase. Tu, Guo, Chen et al. found that the equivalents of YcgC in other bacteria species are also deacetylases; these enzymes therefore represent a new deacetylase family. In the future, the clip-chip approach could be used to discover new members of other enzyme families.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.05322.001
DOI:
10.7554/eLife.05322.002
DOI:
10.7554/eLife.05322.003
DOI:
10.7554/eLife.05322.004
DOI:
10.7554/eLife.05322.005
DOI:
10.7554/eLife.05322.006
DOI:
10.7554/eLife.05322.007
DOI:
10.7554/eLife.05322.008
DOI:
10.7554/eLife.05322.009
DOI:
10.7554/eLife.05322.010
DOI:
10.7554/eLife.05322.011
DOI:
10.7554/eLife.05322.012
DOI:
10.7554/eLife.05322.013
DOI:
10.7554/eLife.05322.014
DOI:
10.7554/eLife.05322.015
DOI:
10.7554/eLife.05322.016
DOI:
10.7554/eLife.05322.017
DOI:
10.7554/eLife.05322.018
DOI:
10.7554/eLife.05322.019
DOI:
10.7554/eLife.05322.020
DOI:
10.7554/eLife.05322.021
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2015
detail.hit.zdb_id:
2687154-3
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