Cellular ATP Levels Determine the Stability of a Nucleotide Kinase.

ABSTRACT: The energy currency of the cell ATP, is used by kinases to drive key cellular processes. However, the connection of cellular ATP abundance and protein stability is still under investigation. Using Fast Relaxation Imaging paired with alanine scanning and ATP depletion experiments, we study the nucleotide kinase (APSK) domain of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) synthase, a marginally stable protein. Here, we show that the in-cell stability of the APSK is determined by ligand binding and directly connected to cellular ATP levels. The observed protein stability change for different ligand-bound states or under ATP-depleted conditions ranges from ΔG_f ⁰ = -10.7 to +13.8 kJ/mol, which is remarkable since it exceeds changes measured previously, for example upon os

SUBMITTER: Brylski O 

PROVIDER: S-EPMC8710738 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature