Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1865, Issue 3, Pages 344-352Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2016.12.002
Keywords
Nitrogen; Ntr; Ribosome; PII; Rmf; ReIE; Persister
Categories
Funding
- CNPq
- Fundacao Araucaria
- CAPES
- National Institute of Science and Technology of Biological Nitrogen Fixation - INCT-FBN
- South-East Health Authority of Norway (Helse Sor-Ost)
- Research Council of Norway
- Oslo University Hospital (OUS)
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Nitrogen is needed for the biosynthesis of biomolecules including proteins and nucleic acids. In the absence of fixed nitrogen prokaryotes such as E. coli immediately ceases growth. Ammonium is the preferred nitrogen source for E. coli supporting the fastest growth rates. Under conditions of ammonium limitation, E. coli can use alternative nitrogen sources to supply ammonium ions and this reprogramming is led by the induction of the NtrC regulon. Here we used label free proteomics to determine the dynamics of E. coli proteins expression in response to ammonium starvation in both the short (30 min) and the longer (60 min) starvation. Protein abundances and post-translational modifications confirmed that activation of the NtrC regulon acts as the first line of defense against nitrogen starvation. The ribosome inactivating protein Rmf was induced shortly after ammonium exhaustion and this was preceded by induction of other ribosome inactivating proteins such as Hpf and RaiA supporting the hypothesis that ribosome shut-down is a key process during nitrogen limitation stress. The proteomic data revealed that growth arrest due to nitrogen starvation correlates with the accumulation of proteins involved in DNA condensation, RNA and protein catabolism and ribosome hibernation. Collectively, these proteome adaptations will result in metabolic inactive cells which are likely to exhibit multidrug tolerance. (C) 2016 Elsevier B.V. All rights reserved.
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