Escherichia coli robustly expresses ATP synthase at growth rate-maximizing concentrations.
FEBS J
; 289(16): 4925-4934, 2022 08.
Article
en En
| MEDLINE
| ID: mdl-35175666
ABSTRACT
Fitness-enhancing adaptations of protein expression and its regulation are an important aspect of bacterial evolution. A key question is whether evolution has led to optimal protein expression that maximizes immediate growth rate (short-term fitness) in a robust manner (consistently across diverse conditions). Alternatively, they could display suboptimal short-term fitness, because they cannot do better or because they instead strive for long-term fitness maximization by, for instance, preparing for future conditions. To address this question, we focus on the ATP-producing enzyme F1 F0 H+ -ATPase, which is an abundant enzyme and ubiquitously expressed across conditions. Its expression is highly regulated and dependent on growth rate and nutrient conditions. For instance, during growth on sugars, when metabolism is overflowing acetate, glycolysis supplies most ATP, while H+ -ATPase is the main source of ATP synthesis during growth on acetate. We tested the optimality of H+ -ATPase expression in Escherichia coli across different nutrient conditions. In all tested conditions, wild-type E. coli expresses its H+ -ATPase remarkably close (within a few per cent) to optimal concentrations that maximize immediate growth rate. This work indicates that bacteria can indeed achieve robust optimal protein expression for immediate growth-rate maximization.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Contexto en salud:
3_ND
Problema de salud:
3_neglected_diseases
/
3_zoonosis
Asunto principal:
ATPasas de Translocación de Protón
/
Escherichia coli
Idioma:
En
Revista:
FEBS J
Asunto de la revista:
BIOQUIMICA
Año:
2022
Tipo del documento:
Article
País de afiliación:
Países Bajos