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Substrate Specificity of the Bacillus subtilis BY-Kinase PtkA Is Controlled by Alternative Activators: TkmA and SalA

Abderahmane Derouiche (Institutionen för biologi och bioteknik, Systembiologi) ; Lei Shi (Institutionen för biologi och bioteknik, Systembiologi) ; Aida Kalantari (Institutionen för biologi och bioteknik, Systembiologi) ; Ivan Mijakovic (Institutionen för biologi och bioteknik, Systembiologi)
Frontiers in Microbiology (1664-302X). Vol. 7 (2016),
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: bacterial protein-tyrosine kinase; protein phosphorylation; kinase specificity; kinase activator; transcription factor


Article Number: 1525



Denna post skapades 2016-10-24. Senast ändrad 2016-11-03.
CPL Pubid: 243988

 

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Institutioner (Chalmers)

Institutionen för biologi och bioteknik, Systembiologi

Ämnesområden

Mikrobiologi

Chalmers infrastruktur