Post-translational regulation of a Porphyromonas gingivalis regulator
Background: Bacteria use two-component signal transduction systems (among others) to perceive and respond to environmental changes. Within the genus Porphyromonas, we observed degeneration of these systems, as exemplified by the loss of RprX, the sensor kinase partner of the RprY. Objective: The pur...
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Online Access: | http://dx.doi.org/10.1080/20002297.2018.1487743 |
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doaj-81a8b171d3464ea0aae2948e39f84d972020-11-25T00:35:05ZengTaylor & Francis GroupJournal of Oral Microbiology2000-22972018-01-0110110.1080/20002297.2018.14877431487743Post-translational regulation of a Porphyromonas gingivalis regulatorYuqing Li0Karthik Krishnan1Margaret J. Duncan2The Forsyth InstituteThe Forsyth InstituteThe Forsyth InstituteBackground: Bacteria use two-component signal transduction systems (among others) to perceive and respond to environmental changes. Within the genus Porphyromonas, we observed degeneration of these systems, as exemplified by the loss of RprX, the sensor kinase partner of the RprY. Objective: The purpose of this study was to investigate modulation of RprY function by acetylation. Design: The transcriptional activity of the rprY-pat genes were measured by RT-PCR and 5ʹ-RACE. The acetylation of RprY were detected by western blotting. Electromobility shift and in vitro ChIP assays were used to measure the DNA binding activity of RprY. The expression of RprY target genes was measured by qRT-PCR. Effects of acetylation on phosphorylation of RprY were measured by Phos-tag gels. Results: The rprY gene is cotranscribed with pat. RprY is acetylated in vivo, and autoacetylated in vitro in a reaction that is enhanced by Pat; the CobB sirtuin deacetylates RprY. Acetylation reduced the DNA binding of RprY. Induced oxidative stress decreased production of RprY in vivo, increased its acetylation and increased expression of nqrA. Conclusions: We propose that to compensate for the loss of RprX, P. gingivalis has evolved a novel mechanism to inactivate RprY through acetylation.http://dx.doi.org/10.1080/20002297.2018.1487743Porphyromonas gingivalisRprYacetylationCobBoxidative response |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yuqing Li Karthik Krishnan Margaret J. Duncan |
spellingShingle |
Yuqing Li Karthik Krishnan Margaret J. Duncan Post-translational regulation of a Porphyromonas gingivalis regulator Journal of Oral Microbiology Porphyromonas gingivalis RprY acetylation CobB oxidative response |
author_facet |
Yuqing Li Karthik Krishnan Margaret J. Duncan |
author_sort |
Yuqing Li |
title |
Post-translational regulation of a Porphyromonas gingivalis regulator |
title_short |
Post-translational regulation of a Porphyromonas gingivalis regulator |
title_full |
Post-translational regulation of a Porphyromonas gingivalis regulator |
title_fullStr |
Post-translational regulation of a Porphyromonas gingivalis regulator |
title_full_unstemmed |
Post-translational regulation of a Porphyromonas gingivalis regulator |
title_sort |
post-translational regulation of a porphyromonas gingivalis regulator |
publisher |
Taylor & Francis Group |
series |
Journal of Oral Microbiology |
issn |
2000-2297 |
publishDate |
2018-01-01 |
description |
Background: Bacteria use two-component signal transduction systems (among others) to perceive and respond to environmental changes. Within the genus Porphyromonas, we observed degeneration of these systems, as exemplified by the loss of RprX, the sensor kinase partner of the RprY. Objective: The purpose of this study was to investigate modulation of RprY function by acetylation. Design: The transcriptional activity of the rprY-pat genes were measured by RT-PCR and 5ʹ-RACE. The acetylation of RprY were detected by western blotting. Electromobility shift and in vitro ChIP assays were used to measure the DNA binding activity of RprY. The expression of RprY target genes was measured by qRT-PCR. Effects of acetylation on phosphorylation of RprY were measured by Phos-tag gels. Results: The rprY gene is cotranscribed with pat. RprY is acetylated in vivo, and autoacetylated in vitro in a reaction that is enhanced by Pat; the CobB sirtuin deacetylates RprY. Acetylation reduced the DNA binding of RprY. Induced oxidative stress decreased production of RprY in vivo, increased its acetylation and increased expression of nqrA. Conclusions: We propose that to compensate for the loss of RprX, P. gingivalis has evolved a novel mechanism to inactivate RprY through acetylation. |
topic |
Porphyromonas gingivalis RprY acetylation CobB oxidative response |
url |
http://dx.doi.org/10.1080/20002297.2018.1487743 |
work_keys_str_mv |
AT yuqingli posttranslationalregulationofaporphyromonasgingivalisregulator AT karthikkrishnan posttranslationalregulationofaporphyromonasgingivalisregulator AT margaretjduncan posttranslationalregulationofaporphyromonasgingivalisregulator |
_version_ |
1725310401972797440 |