Premium
Determining ClpXP Substrates Under Different Nutrient Conditions in Escherichia coli
Author(s) -
Peterson Celeste,
Mendes Amberely,
Lambert Adrian,
Papaj Agllai,
Ngo Pauline,
Von Rosen Tatjana
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.918.17
Subject(s) - protease , escherichia coli , biology , starvation , biochemistry , enzyme , microbiology and biotechnology , gene , endocrinology
Cellular protein concentrations reflect a balance between synthesis, degradation, and dilution by cell growth. Synthesis is routinely analyzed in high‐throughput experiments, but fewer studies consider degradation, particularly under non‐optimal growth conditions such as starvation. ClpXP is a central and conserved protease that degrades numerous proteins. Here, we modified the ClpXP protease trap assay to identify which proteins are degraded under glucose and no glucose conditions. Substrates involved in replication, protein synthesis, and metabolism were found to be associated with ClpXP during starvation. Conversely, substrates involved in the stress response were more likely to be degraded in glucose conditions. Almost all of these proteins had a canonical C or N terminal ClpX tag on them. Thus, the ClpXP protease markedly remodels its substrate profile during starvation. Support or Funding Information Research Corporation for Scientific Advancement