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Front Cover: An Integrated Proteomic Approach Uncovers Novel Substrates and Functions of the Lon Protease in Escherichia coli
Author(s) -
Arends Jan,
Griego Marcena,
Thomanek Nikolas,
Lindemann Claudia,
Kutscher Blanka,
Meyer Helmut E.,
Narberhaus Franz
Publication year - 2018
Publication title -
proteomics
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201870111
Subject(s) - protease , proteolysis , escherichia coli , proteome , proteomics , biology , biochemistry , proteases , computational biology , substrate specificity , chemistry , microbiology and biotechnology , enzyme , gene
DOI: 10.1002/pmic.201800080 Regulated proteolysis of active and natively folded proteins is a universal strategy to shape the cellular proteome. In article number 1800080 , Arends et al. use a combination of quantitative comparative proteomics and trapping experiments with a proteolytically inactive protease variant to investigate the substrate repertoire of the Lon protease from Escherichia coli . By these approaches, several new physiological functions of the Lon protease are identified.