Higher order assembling of the mycobacterial polar growth factor DivIVA/Wag31.

Choukate, Komal and Gupta, Aanchal and Basu, Brohmomoy and Virk, Karman and Ganguli, Munia and Chaudhuri, Barnali (2019) Higher order assembling of the mycobacterial polar growth factor DivIVA/Wag31. Journal of structural biology. p. 107429. ISSN 1095-8657

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Abstract

DivIVA or Wag31, which is an essential pole organizing protein in mycobacteria, can self-assemble at the negatively curved side of the membrane at the growing pole to form a higher order structural scaffold for maintaining cellular morphology and localizing various target proteins for cell-wall biogenesis. The structural organization of polar scaffold formed by polymerization of coiled-coil rich Wag31, which is implicated in the anti-tubercular activities of amino-pyrimidine sulfonamides, remains to be determined. A single-site phosphorylation in Wag31 regulates peptidoglycan biosynthesis in mycobacteria. We report biophysical characterizations of filaments formed by mycobacterial Wag31 using circular dichroism, atomic force microscopy and small angle solution X-ray scattering. Atomic force microscopic images of the wild-type, a phospho-mimetic (T73E) and a phospho-ablative (T73A) form of Wag31 show mostly linear filament formation with occasional curving, kinking and apparent branching. Solution X-ray scattering data indicates that the phospho-mimetic forms of the Wag31 polymers are on average more compact than their phospho-ablative counterparts, which is likely due to the extent of bending/branching. Observed structural features in this first view of Wag31 filaments suggest a basis for higher order Wag31 scaffold formation at the pole.

Item Type: Article
Additional Information: Copyright of this article belongs to Elsevier Science
Uncontrolled Keywords: AFM; DivIVA; Mycobacterial growth; SAXS; Wag31 filament; bacterial polar growth
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 06 Dec 2019 15:41
Last Modified: 06 Dec 2019 15:41
URI: http://crdd.osdd.net/open/id/eprint/2503

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