LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Prabhjot Kaur, Marvin Rausch, Basanti Malakar, Uchenna Watson, Nikhil P. Damle, Yogesh Chawla, Sandhya Srinivasan, Kanika Sharma, Tanja Schneider, Gagan Deep Jhingan, Deepak Saini, Debasisa Mohanty, Fabian Grein, Vinay Kumar Nandicoori

ABSTRACT

The Mycobacterium tuberculosis kinase PknB is essential for growth and survival of the pathogen in vitro and in vivo. Here we report the results of our efforts to elucidate the mechanism of regulation of PknB activity. The specific residues in the PknB extracytoplasmic domain that are essential for ligand interaction and survival of the bacterium are identified. The extracytoplasmic domain interacts with mDAP-containing LipidII, and this is abolished upon mutation of the ligand-interacting residues. Abrogation of ligand-binding or sequestration of the ligand leads to aberrant localization of PknB. Contrary to the prevailing hypothesis, abrogation of ligand-binding is linked to activation loop hyperphosphorylation, and indiscriminate hyperphosphorylation of PknB substrates as well as other proteins, ultimately causing loss of homeostasis and cell death. We propose that the ligand-kinase interaction directs the appropriate localization of the kinase, coupled to stringently controlled activation of PknB, and consequently the downstream processes thereof. More... »

PAGES

1231

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-09223-9

DOI

http://dx.doi.org/10.1038/s41467-019-09223-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112760719

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30874556


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