Functional characterization of a novel Mn2+ dependent protein serine/threonine kinase KpnK, produced by Klebsiella pneumoniae strain MGH78578
Autor: | Manjunath Venkataramaiah, Vasanth Vaidyanathan, Govindan Rajamohan, Vijaya Bharathi Srinivasan, Amitabha Mondal |
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Jazyk: | angličtina |
Předmět: |
Cations
Divalent Klebsiella pneumoniae Molecular Sequence Data Coenzymes Biophysics Gene Expression Microbial Sensitivity Tests Protein Serine-Threonine Kinases Antimicrobial resistance Biochemistry Microbiology Serine Bacterial Proteins Stress Physiological Structural Biology Ser/Thr kinase Drug Resistance Multiple Bacterial Escherichia coli Genetics Phosphorylation Threonine Molecular Biology Serine/threonine-specific protein kinase Manganese Base Sequence biology Kinase Autophosphorylation Cell Biology Hydrogen-Ion Concentration biology.organism_classification Recombinant Proteins Anti-Bacterial Agents Cephalosporins Imipenem Nosocomial pathogen Signal transduction Gene Deletion Signal Transduction |
Zdroj: | FEBS Letters. (21):3778-3786 |
ISSN: | 0014-5793 |
DOI: | 10.1016/j.febslet.2012.09.007 |
Popis: | Klebsiella pneumoniae MGH78578 contains ∼500 uncharacterized signaling proteins and in this study, we characterized the biological functions of a novel eukaryotic-like serine/threonine kinase; ESTK (KpnK). Studies demonstrated that KpnK undergoes autophosphorylation within the pH range 7.0–7.5 at 37°C in a time- and concentration- dependent manner, with Mn2+ as its cofactor. The ΔkpnK mutant exhibited higher sensitivity to gastrointestinal and oxidative stresses. Deletion of kpnK resulted in a two to threefold increased susceptibility towards imipenem, cefepime, ceftriaxone and ceftazidime. Our study has provided overall evidence for the involvement of ESTK in regulating bacterial physiology, stress response and drug resistance. This report has unmasked the occurrence of Ser/Thr kinase mediated signaling for the first time in K. pneumoniae.Structured summary of protein interactionsKpnK phosphorylates KpnK by protein kinase assay (View interaction). |
Databáze: | OpenAIRE |
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