The lipoprotein DolP affects cell separation in Escherichia coli, but not as an upstream regulator of NlpD.
The lipoprotein DolP affects cell separation in Escherichia coli, but not as an upstream regulator of NlpD.
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脂蛋白 DolP 影响大肠杆菌中的细胞分离,但不是 NlpD 的上游调节因子。
DOI:
10.1099/mic.0.001197
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发表时间:
2022
期刊:
影响因子:
--
通讯作者:
Boelter G
中科院分区:
文献类型:
--
作者:
Boelter G
Bacterial amidases are essential to split the shared envelope of adjunct daughter cells to allow cell separation. Their activity needs to be precisely controlled to prevent cell lysis. InEscherichia coli,amidase activity is controlled by three regulatory proteins NlpD, EnvC and ActS. However, recent studies linked the outer membrane lipoprotein DolP (formerly YraP) as a potential upstream regulator of NlpD. In this study we explored this link in further detail. To our surprise DolP did not modulate amidase activityin vitroand was unable to interact with NlpD in pull-down and MST (MicroScale Thermophoresis) assays. Next, we excluded the hypothesis that ΔdolPphenocopied ΔnlpDin a range of envelope stresses. However, morphological analysis of double deletion mutants of amidases (AmiA, AmiB AmiC) and amidase regulators withdolPrevealed that ΔamiAΔdolPand ΔenvCΔdolPmutants display longer chain length compared to their parental strains indicating a role for DolP in cell division. Overall, we present evidence that DolP does not affect NlpD functionin vitro, implying that DolP is not an upstream regulator of NlpD. However, DolP may impact daughter cell separation by interacting directly with AmiA or AmiC, or by a yet undiscovered mechanism.
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DOI:
10.1073/pnas.120163297
发表时间:
2000-06-06
影响因子:
11.1
作者:
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通讯作者:
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DOI:
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发表时间:
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期刊:
bioRxiv
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