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Identification and Molecular Characterization of YsaL (Ye3555): A Novel Negative Regulator of YsaN ATPase in Type Three Secretion System of Enteropathogenic Bacteria Yersinia enterocolitica

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Title Identification and Molecular Characterization of YsaL
(Ye3555): A Novel Negative Regulator of YsaN ATPase in
Type Three Secretion System of Enteropathogenic
Bacteria Yersinia enterocolitica
 
Creator Chatterjee, Rakesh
Halder, Pranab Kumar
Datta, Saumen
 
Subject Structural Biology & Bioinformatics
 
Description Type Three Secretion (T3S) ATPases are involved in delivery of virulent factors from bacteria to their hosts (through
injectisome) in an energy (ATP) dependent manner during pathogenesis. The activities of these ATPases are tightly
controlled by their specific regulators. In Yersinia enterocolitica, YsaN was predicted as a putative ATPase of the Ysa-Ysp Type Three Secretion System (T3SS) based on sequence similarity with other T3S ATPases. However detailed study and characterization of YsaN and its regulation remains largely obscure. Here, in this study, we have successfully cloned, overexpressed,purified and characterized the molecular properties of YsaN from Yersinia enterocolitica. YsaN acts as a Mg2+ dependent ATPase and exists in solution as higher order oligomer (dodecamer). The ATPase activity of oligomeric YsaN is
several fold higher than the monomeric form. Furthermore, by employing in silico studies we have identified the existence of a negative regulator of YsaN- a hypothetical protein YE3555 (termed ‘YsaL’). To verify the functionality of YsaL, we have evaluated the biochemical and biophysical properties of YsaL. Purified YsaL is dimeric in solution and strongly associates with YsaN to form a stable heterotrimeric YsaL-YsaN complex (stoichiometry- 2:1). The N terminal 6–20 residues of YsaN are invariably required for stable YsaL-YsaN complex formation. YsaL inhibited the ATPase activity of YsaN with a maximum inhibition at the molar ratio 2:1 (YsaL: YsaN). In short, our studies provide an insight into the presence of YsaN ATPase in Yersinia enterocolitica and its regulator YsaL. Our studies also correlate the functionality of one of the existing protein
interaction networks that possibly is indispensable for the energy dependent process of Ysa-Ysp T3SS in pathogenic Yersinia enterocolitica
 
Date 2013-10
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2426/1/Jana_et_al%2D2013%2DMacromolecular_Bioscience.pdf
Chatterjee, Rakesh and Halder, Pranab Kumar and Datta, Saumen (2013) Identification and Molecular Characterization of YsaL (Ye3555): A Novel Negative Regulator of YsaN ATPase in Type Three Secretion System of Enteropathogenic Bacteria Yersinia enterocolitica. PLOS ONE, 8 (10). e75028.
 
Relation http://www.eprints.iicb.res.in/2426/