Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved]
The two-component system LytSR has been linked to the signal transduction of cell membrane electrical potential perturbation and is involved in the adaptation of Staphylococcus aureus to cationic antimicrobial peptides. It consists of a membrane-bound histidine kinase, LytS, which belongs to the fam...
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| Format: | Article |
| Language: | English |
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F1000 Research Ltd
2016-03-01
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| Series: | F1000Research |
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| Online Access: | http://f1000research.com/articles/4-79/v2 |
| _version_ | 1818284192867287040 |
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| author | Kevin Patel Dasantila Golemi-Kotra |
| author_facet | Kevin Patel Dasantila Golemi-Kotra |
| author_sort | Kevin Patel |
| collection | DOAJ |
| description | The two-component system LytSR has been linked to the signal transduction of cell membrane electrical potential perturbation and is involved in the adaptation of Staphylococcus aureus to cationic antimicrobial peptides. It consists of a membrane-bound histidine kinase, LytS, which belongs to the family of multiple transmembrane-spanning domains receptors, and a response regulator, LytR, which belongs to the novel family of non-helix-turn-helix DNA-binding domain proteins. LytR regulates the expression of cidABC and lrgAB operons, the gene products of which are involved in programmed cell death and lysis. In vivo studies have demonstrated involvement of two overlapping regulatory networks in regulating the lrgAB operon, both depending on LytR. One regulatory network responds to glucose metabolism and the other responds to changes in the cell membrane potential. Herein, we show that LytS has autokinase activity and can catalyze a fast phosphotransfer reaction, with 50% of its phosphoryl group lost within 1 minute of incubation with LytR. LytS has also phosphatase activity. Notably, LytR undergoes phosphorylation by acetyl phosphate at a rate that is 2-fold faster than the phosphorylation by LytS. This observation is significant in lieu of the in vivo observations that regulation of the lrgAB operon is LytR-dependent in the presence of excess glucose in the medium. The latter condition does not lead to perturbation of the cell membrane potential but rather to the accumulation of acetate in the cell. Our study provides insights into the molecular basis for regulation of lrgAB in a LytR-dependent manner under conditions that do not involve sensing by LytS. |
| first_indexed | 2024-12-13T00:48:54Z |
| format | Article |
| id | doaj.art-81b89d9c184442b3858576a6c8725e40 |
| institution | Directory Open Access Journal |
| issn | 2046-1402 |
| language | English |
| last_indexed | 2024-12-13T00:48:54Z |
| publishDate | 2016-03-01 |
| publisher | F1000 Research Ltd |
| record_format | Article |
| series | F1000Research |
| spelling | doaj.art-81b89d9c184442b3858576a6c8725e402022-12-22T00:04:57ZengF1000 Research LtdF1000Research2046-14022016-03-01410.12688/f1000research.6213.28994Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved]Kevin Patel0Dasantila Golemi-Kotra1Department of Chemistry, York University, Toronto, Toronto, Ontario, M3J 1P3, CanadaDepartment of Biology, York University, Toronto, Toronto, Ontario, M3J 1P3, CanadaThe two-component system LytSR has been linked to the signal transduction of cell membrane electrical potential perturbation and is involved in the adaptation of Staphylococcus aureus to cationic antimicrobial peptides. It consists of a membrane-bound histidine kinase, LytS, which belongs to the family of multiple transmembrane-spanning domains receptors, and a response regulator, LytR, which belongs to the novel family of non-helix-turn-helix DNA-binding domain proteins. LytR regulates the expression of cidABC and lrgAB operons, the gene products of which are involved in programmed cell death and lysis. In vivo studies have demonstrated involvement of two overlapping regulatory networks in regulating the lrgAB operon, both depending on LytR. One regulatory network responds to glucose metabolism and the other responds to changes in the cell membrane potential. Herein, we show that LytS has autokinase activity and can catalyze a fast phosphotransfer reaction, with 50% of its phosphoryl group lost within 1 minute of incubation with LytR. LytS has also phosphatase activity. Notably, LytR undergoes phosphorylation by acetyl phosphate at a rate that is 2-fold faster than the phosphorylation by LytS. This observation is significant in lieu of the in vivo observations that regulation of the lrgAB operon is LytR-dependent in the presence of excess glucose in the medium. The latter condition does not lead to perturbation of the cell membrane potential but rather to the accumulation of acetate in the cell. Our study provides insights into the molecular basis for regulation of lrgAB in a LytR-dependent manner under conditions that do not involve sensing by LytS.http://f1000research.com/articles/4-79/v2Cell SignalingControl of Gene Expression |
| spellingShingle | Kevin Patel Dasantila Golemi-Kotra Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved] F1000Research Cell Signaling Control of Gene Expression |
| title | Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved] |
| title_full | Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved] |
| title_fullStr | Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved] |
| title_full_unstemmed | Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved] |
| title_short | Signaling mechanism by the Staphylococcus aureus two-component system LytSR: role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS [version 2; referees: 2 approved] |
| title_sort | signaling mechanism by the staphylococcus aureus two component system lytsr role of acetyl phosphate in bypassing the cell membrane electrical potential sensor lyts version 2 referees 2 approved |
| topic | Cell Signaling Control of Gene Expression |
| url | http://f1000research.com/articles/4-79/v2 |
| work_keys_str_mv | AT kevinpatel signalingmechanismbythestaphylococcusaureustwocomponentsystemlytsrroleofacetylphosphateinbypassingthecellmembraneelectricalpotentialsensorlytsversion2referees2approved AT dasantilagolemikotra signalingmechanismbythestaphylococcusaureustwocomponentsystemlytsrroleofacetylphosphateinbypassingthecellmembraneelectricalpotentialsensorlytsversion2referees2approved |