RT Journal Article SR Electronic(1) A1 Gupta, Shamba A1 Banerjee, Srijon Kaushik A1 Chatterjee, Ayan A1 Sharma, Arun Kumar A1 Kundu, Manikuntala A1 Basu, JoyotiYR 2015 T1 Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division JF Microbiology, VO 161 IS 8 SP 1627 OP 1638 DO https://doi.org/10.1099/mic.0.000108 PB Microbiology Society, SN 1465-2080, AB Coordinated bacterial cell septation and cell wall biosynthesis require formation of protein complexes at the sites of division and elongation, in a temporally controlled manner. The protein players in these complexes remain incompletely understood in mycobacteria. Using in vitro and in vivo assays, we showed that Rv2147c (or SepF) of Mycobacterium tuberculosis interacts with the principal driver of cytokinesis, FtsZ. SepF also interacts with itself both in vitro and in vivo. Amino acid residues 189A, 190K and 215F are required for FtsZ–SepF interaction, and are conserved across Gram-positive bacteria. Using Mycobacterium smegmatis as a surrogate system, we confirmed that sepF MSMEG is essential. Knockdown of SepF led to cell elongation, defective growth and failure of FtsZ to localize to the site of division, suggesting that SepF assists FtsZ localization at the site of division. Furthermore, SepF interacted with MurG, a peptidoglycan-synthesizing enzyme, both in vitro and in vivo, suggesting that SepF could serve as a link between cell division and peptidoglycan synthesis. SepF emerges as a newly identified essential component of the cell division complex in mycobacteria., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000108