Substrate Specificity of the Bacillus subtilis BY-Kinase PtkA Is Controlled by Alternative Activators: TkmA and SalA
Artikel i vetenskaplig tidskrift, 2016

Bacterial protein-tyrosine kinases (BY-kinases) are known to regulate different aspects of bacterial physiology, by phosphorylating cellular protein substrates. Physiological cues that trigger BY-kinases activity are largely unexplored. In Proteobacteria, BY-kinases contain a cytosol-exposed catalytic domain and a transmembrane activator domain in a single polypeptide chain. In Firrnicutes, the BY-kinase catalytic domain and the transmembrane activator domain exist as separate polypeptides. We have previously speculated that this architecture might enable the Firmicutes BY-kinases to interact with alternative activators, and thus account for the observed ability of these kinases to phosphorylate several distinct classes of protein substrates. Here, we present experimental evidence that supports this hypothesis. We focus on the model Firmicute-type BY-kinase PtkA from Bacillus subtilis, known to phosphorylate several different protein substrates. We demonstrate that the transcriptional regulator SaIA, hitherto known as a substrate of PtkA, can also act as a PtkA activator. In doing so, SaIA competes with the canonical PtkA activator, TkmA. Our results suggest that the respective interactions of SaIA and TkmA with PtkA favor phosphorylation of different protein substrates in vivo and in vitro. This observation may contribute to explaining how specificity is established in the seemingly promiscuous interactions of BY-kinases with their cellular substrates.

transcription factor

kinase activator

kinase specificity

bacterial protein-tyrosine kinase

protein phosphorylation


Abderahmane Derouiche

Chalmers, Biologi och bioteknik, Systembiologi

Lei Shi

Chalmers, Biologi och bioteknik, Systembiologi

Aida Kalantari

Chalmers, Biologi och bioteknik, Systembiologi

Ivan Mijakovic

Chalmers, Biologi och bioteknik, Systembiologi

Frontiers in Microbiology

1664302x (eISSN)

Vol. 7 SEP 1525





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