Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli.
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 '...
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doaj-00c0a0d210d54bceaa818ba64b90d9572020-11-25T00:05:48ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01102e011782310.1371/journal.pone.0117823Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli.Jin JinRuijuan WuJia ZhuShaoyuan YangZhen LeiNan WangVinay K SinghJimin ZhengZongchao JiaYhdE, 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.http://europepmc.org/articles/PMC4319933?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jin Jin Ruijuan Wu Jia Zhu Shaoyuan Yang Zhen Lei Nan Wang Vinay K Singh Jimin Zheng Zongchao Jia |
spellingShingle |
Jin Jin Ruijuan Wu Jia Zhu Shaoyuan Yang Zhen Lei Nan Wang Vinay K Singh Jimin Zheng Zongchao Jia Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli. PLoS ONE |
author_facet |
Jin Jin Ruijuan Wu Jia Zhu Shaoyuan Yang Zhen Lei Nan Wang Vinay K Singh Jimin Zheng Zongchao Jia |
author_sort |
Jin Jin |
title |
Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli. |
title_short |
Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli. |
title_full |
Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli. |
title_fullStr |
Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli. |
title_full_unstemmed |
Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli. |
title_sort |
insights into the cellular function of yhde, a nucleotide pyrophosphatase from escherichia coli. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2015-01-01 |
description |
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. |
url |
http://europepmc.org/articles/PMC4319933?pdf=render |
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