Higher order assembling of the mycobacterial polar growth factor DivIVA/Wag31 |
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| Affiliation: | 1. CSIR Institute of Microbial Technology, Chandigarh, India;2. CSIR Institute of Genomics and Integrative Biology, New Delhi, India;3. Academy of Scientific and Innovative Research (AcSIR), Anusandhan Bhawan, 2 Rafi Marg, New Delhi 110001, India;1. Biomedical Research, The University of Texas Health Science Center @ Tyler, Tyler, TX 75708, USA;1. Department of Microbiology and Immunology, Weill Cornell Medical College, New York, NY 10065, USA;2. Department of Computer Science and Engineering, Texas A&M University, USA;3. Department of Medicine, Weill Cornell Medical College, New York, NY 10065, USA;4. Department of Biochemistry and Biophysics, Texas A&M University, USA;1. Department of Bioengineering, Stanford University, Stanford, CA 94305, USA;2. Biophysics Program, Stanford University, Stanford, CA 94305, USA;3. Stanford Shared FACS Facility, Stanford University School of Medicine, Stanford, CA 94305, USA;4. Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA |
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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. |
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| Keywords: | Mycobacterial growth Bacterial polar growth DivIVA Wag31 filament AFM SAXS |
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