%0 Journal Article %1 wenkUniversallyConservedATPase2012 %A Wenk, Meike %A Ba, Qiaorui %A Erichsen, Veronika %A MacInnes, Katherine %A Wiese, Heike %A Warscheid, Bettina %A Koch, Hans-Georg %C United States %D 2012 %J The Journal of biological chemistry %K Adenosine Peroxide/*pharmacology,Oxidants/*pharmacology,Oxidative Post-Translational/drug Processing Proteins/genetics/*metabolism,Escherichia Proteins/genetics/metabolism,Humans,Hydrogen Proteins/genetics/metabolism,to_read Stress/*drug Triphosphatases/genetics/*metabolism,Catalase/genetics/metabolism,Escherichia coli coli/genetics/*metabolism,GTP-Binding effects/genetics,Phosphorylation/drug effects/genetics,Protein effects/genetics,Repressor %N 52 %P 43585--43598 %R 10.1074/jbc.M112.413070 %T A Universally Conserved ATPase Regulates the Oxidative Stress Response in Escherichia Coli. %V 287 %X YchF is an evolutionarily conserved ATPase of unknown function. In humans, the YchF homologue hOla1 appears to influence cell proliferation and was found to be up-regulated in many tumors. A possible involvement in regulating the oxidative stress response was also suggested, but details on the underlying mechanism are lacking. For gaining insight into YchF function, we used Escherichia coli as a model organism and found that YchF overexpression resulted in H(2)O(2) hypersensitivity. This was not caused by transcriptional or translational down-regulation of H(2)O(2)-scavenging enzymes. Instead, we observed YchF-dependent inhibition of catalase activity and a direct interaction with the major E. coli catalase KatG. KatG inhibition was dependent on the ATPase activity of YchF and was regulated by post-translational modifications, most likely including an H(2)O(2)-dependent dephosphorylation. We furthermore showed that YchF expression is repressed by the transcription factor OxyR and further post-translationally modified in response to H(2)O(2). In summary, our data show that YchF functions as a novel negative regulator of the oxidative stress response in E. coli. Considering the available data on hOla1, YchF/Ola1 most likely execute similar functions in bacteria and humans, and their up-regulation inhibits the ability of the cells to scavenge damaging reactive oxygen species.

@article{wenkUniversallyConservedATPase2012, abstract = {YchF is an evolutionarily conserved ATPase of unknown function. In humans, the YchF homologue hOla1 appears to influence cell proliferation and was found to be up-regulated in many tumors. A possible involvement in regulating the oxidative stress response was also suggested, but details on the underlying mechanism are lacking. For gaining insight into YchF function, we used Escherichia coli as a model organism and found that YchF overexpression resulted in H(2)O(2) hypersensitivity. This was not caused by transcriptional or translational down-regulation of H(2)O(2)-scavenging enzymes. Instead, we observed YchF-dependent inhibition of catalase activity and a direct interaction with the major E. coli catalase KatG. KatG inhibition was dependent on the ATPase activity of YchF and was regulated by post-translational modifications, most likely including an H(2)O(2)-dependent dephosphorylation. We furthermore showed that YchF expression is repressed by the transcription factor OxyR and further post-translationally modified in response to H(2)O(2). In summary, our data show that YchF functions as a novel negative regulator of the oxidative stress response in E. coli. Considering the available data on hOla1, YchF/Ola1 most likely execute similar functions in bacteria and humans, and their up-regulation inhibits the ability of the cells to scavenge damaging reactive oxygen species.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {United States}, author = {Wenk, Meike and Ba, Qiaorui and Erichsen, Veronika and MacInnes, Katherine and Wiese, Heike and Warscheid, Bettina and Koch, Hans-Georg}, biburl = {https://www.bibsonomy.org/bibtex/2708cac8ee1174a072b4ea44fc9278630/warscheidlab}, doi = {10.1074/jbc.M112.413070}, interhash = {49d373c8680daf93476085d6f0db5583}, intrahash = {708cac8ee1174a072b4ea44fc9278630}, issn = {1083-351X 0021-9258}, journal = {The Journal of biological chemistry}, keywords = {Adenosine Peroxide/*pharmacology,Oxidants/*pharmacology,Oxidative Post-Translational/drug Processing Proteins/genetics/*metabolism,Escherichia Proteins/genetics/metabolism,Humans,Hydrogen Proteins/genetics/metabolism,to_read Stress/*drug Triphosphatases/genetics/*metabolism,Catalase/genetics/metabolism,Escherichia coli coli/genetics/*metabolism,GTP-Binding effects/genetics,Phosphorylation/drug effects/genetics,Protein effects/genetics,Repressor}, langid = {english}, month = dec, number = 52, pages = {43585--43598}, pmcid = {PMC3527945}, pmid = {23139412}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {A Universally Conserved {{ATPase}} Regulates the Oxidative Stress Response in {{Escherichia}} Coli.}, volume = 287, year = 2012 }