Abstract
YhdE, a Maf-like protein in Escherichia coli, exhibits nucleotide pyrophosphatase (PPase) activity, yet its cellular function remains unknown. Here, we characterized the PPase activity of YhdE on dTTP, UTP and TTP and determined two crystal structures of YhdE, revealing ‘closed’ and ‘open’ conformations of an adaptive active site. Our functional studies demonstrated that YhdE retards cell growth by prolonging the lag and log phases, particularly under stress conditions. Morphology studies showed that yhdE-knockout cells transformed the normal rod shape of wild-type cells to a more spherical form, and the cell wall appeared to become more flexible. In contrast, YhdE overexpression resulted in filamentous cells. This study reveals the previously unknown involvement of YhdE in cell growth inhibition under stress conditions, cell-division arrest and cell-shape maintenance, highlighting YhdE’s important role in E. coli cell-cycle checkpoints.
Highlights
Maf proteins are part of a large family of conserved proteins found in bacteria, archaea and eukaryotes
Previous genetic experiments showed that introduction of the maf gene on a multi-copy plasmid into Bacillus subtilis resulted in extensive filamentation and inhibition of cell division [1], but the biochemical basis for the septation inhibition remains elusive
To further explore the cellular function of YhdE, we examined the influence of the yhdE gene in cell growth under varying conditions and investigated the corresponding changes in cell morphology
Summary
Maf (multicopy associated filamentation) proteins are part of a large family of conserved proteins found in bacteria, archaea and eukaryotes. This family is implicated in the regulation of cell division, their exact cellular function remains unknown. Previous genetic experiments showed that introduction of the maf gene on a multi-copy plasmid into Bacillus subtilis resulted in extensive filamentation and inhibition of cell division [1], but the biochemical basis for the septation inhibition remains elusive. Recent work on a Maf protein from B. subtilis indicated that the inhibition of cell division was associated with DNA transformation and repair [2].
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