Unknown

Dataset Information

0

Viscosity-dependent control of protein synthesis and degradation.


ABSTRACT: It has been proposed that the concentration of proteins in the cytoplasm maximizes the speed of important biochemical reactions. Here we have used Xenopus egg extracts, which can be diluted or concentrated to yield a range of cytoplasmic protein concentrations, to test the effect of cytoplasmic concentration on mRNA translation and protein degradation. We find that protein synthesis rates are maximal in ~1x cytoplasm, whereas protein degradation continues to rise to a higher optimal concentration of ~1.8x. We show that this difference in optima can be attributed to a greater sensitivity of translation to cytoplasmic viscosity. The different concentration optima could produce a negative feedback homeostatic system, where increasing the cytoplasmic protein concentration above the 1x physiological level increases the viscosity of the cytoplasm, which selectively inhibits translation and drives the system back toward the 1x set point.

SUBMITTER: Chen Y 

PROVIDER: S-EPMC10923802 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Viscosity-dependent control of protein synthesis and degradation.

Chen Yuping Y   Huang Jo-Hsi JH   Phong Connie C   Ferrell James E JE  

Nature communications 20240308 1


It has been proposed that the concentration of proteins in the cytoplasm maximizes the speed of important biochemical reactions. Here we have used Xenopus egg extracts, which can be diluted or concentrated to yield a range of cytoplasmic protein concentrations, to test the effect of cytoplasmic concentration on mRNA translation and protein degradation. We find that protein synthesis rates are maximal in ~1x cytoplasm, whereas protein degradation continues to rise to a higher optimal concentratio  ...[more]

Similar Datasets

| S-EPMC10168264 | biostudies-literature
| S-EPMC11963982 | biostudies-literature
| S-EPMC6098157 | biostudies-literature
| S-EPMC4938640 | biostudies-literature
| S-EPMC10173458 | biostudies-literature
| S-EPMC7034999 | biostudies-literature
| S-EPMC3926196 | biostudies-literature