Enzyme expression kinetics by Escherichia coli during transition from rich to minimal media depends on proteome reserves
METADATA ONLY
Loading...
Author / Producer
Date
2023-02
Publication Type
Journal Article
ETH Bibliography
yes
Citations
Altmetric
METADATA ONLY
Data
Rights / License
Abstract
Bacterial fitness depends on adaptability to changing environments. In rich growth medium, which is replete with amino acids, Escherichia coli primarily expresses protein synthesis machineries, which comprise ~40% of cellular proteins and are required for rapid growth. Upon transition to minimal medium, which lacks amino acids, biosynthetic enzymes are synthesized, eventually reaching ~15% of cellular proteins when growth fully resumes. We applied quantitative proteomics to analyse the timing of enzyme expression during such transitions, and established a simple positive relation between the onset time of enzyme synthesis and the fractional enzyme ‘reserve’ maintained by E. coli while growing in rich media. We devised and validated a coarse-grained kinetic model that quantitatively captures the enzyme recovery kinetics in different pathways, solely on the basis of proteomes immediately preceding the transition and well after its completion. Our model enables us to infer regulatory strategies underlying the ‘as-needed’ gene expression programme adopted by E. coli.
Permanent link
Publication status
published
External links
Editor
Book title
Journal / series
Volume
8 (2)
Pages / Article No.
347 - 359
Publisher
Nature
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
Organisational unit
Notes
Funding
670821 - Proteomics 4D: The proteome in context (EC)