Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues
Bacteria possess protein serine/threonine and tyrosine kinases which resemble eukaryal kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the analogy might extend further, and bacterial kinases may also undergo mutual phosphorylation and activation, which is current...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2014-09-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2014.00495/full |
| _version_ | 1818549756706684928 |
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| author | Lei eShi Nathalie ePigeonneau Vaishnavi eRavikumar Paula eDobrinic Boris eMacek Damjan eFranjevic Marie-Françoise eNoirot-gros Ivan eMijakovic |
| author_facet | Lei eShi Nathalie ePigeonneau Vaishnavi eRavikumar Paula eDobrinic Boris eMacek Damjan eFranjevic Marie-Françoise eNoirot-gros Ivan eMijakovic |
| author_sort | Lei eShi |
| collection | DOAJ |
| description | Bacteria possess protein serine/threonine and tyrosine kinases which resemble eukaryal kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the analogy might extend further, and bacterial kinases may also undergo mutual phosphorylation and activation, which is currently considered as a hallmark of eukaryal kinase networks. In order to test this hypothesis, we explored the capacity of all members of four different classes of serine/threonine and tyrosine kinases present in the firmicute model organism Bacillus subtilis to phosphorylate each other in vitro and interact with each other in vivo. The interactomics data suggested a high degree of connectivity among all types of kinases, while phosphorylation assays revealed equally wide-spread cross-phosphorylation events. Our findings suggest that the Hanks-type kinases PrkC, PrkD and YabT exhibit the highest capacity to phosphorylate other B. subtilis kinases, while the BY-kinase PtkA and the two-component-like kinases RsbW and SpoIIAB show the highest propensity to be phosphorylated by other kinases. Analysis of phosphorylated residues on several selected recipient kinases suggests that most cross-phosphorylation events concern key regulatory residues. Therefore, cross-phosphorylation events are very likely to influence the capacity of recipient kinases to phosphorylate substrates downstream in the signal transduction cascade. We therefore conclude that bacterial serine/threonine and tyrosine kinases probably engage in a network-type behavior previously described only in eukaryal cells. |
| first_indexed | 2024-12-12T08:37:26Z |
| format | Article |
| id | doaj.art-01051366fa4d4713a5997977ed98b1d3 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-12T08:37:26Z |
| publishDate | 2014-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-01051366fa4d4713a5997977ed98b1d32022-12-22T00:30:53ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2014-09-01510.3389/fmicb.2014.00495110981Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residuesLei eShi0Nathalie ePigeonneau1Vaishnavi eRavikumar2Paula eDobrinic3Boris eMacek4Damjan eFranjevic5Marie-Françoise eNoirot-gros6Ivan eMijakovic7Chalmers University of TechnologyInstitut National de Recherche AgronomiqueUniversity of TübingenZagreb UniversityUniversity of TübingenZagreb UniversityInstitut National de Recherche AgronomiqueChalmers University of TechnologyBacteria possess protein serine/threonine and tyrosine kinases which resemble eukaryal kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the analogy might extend further, and bacterial kinases may also undergo mutual phosphorylation and activation, which is currently considered as a hallmark of eukaryal kinase networks. In order to test this hypothesis, we explored the capacity of all members of four different classes of serine/threonine and tyrosine kinases present in the firmicute model organism Bacillus subtilis to phosphorylate each other in vitro and interact with each other in vivo. The interactomics data suggested a high degree of connectivity among all types of kinases, while phosphorylation assays revealed equally wide-spread cross-phosphorylation events. Our findings suggest that the Hanks-type kinases PrkC, PrkD and YabT exhibit the highest capacity to phosphorylate other B. subtilis kinases, while the BY-kinase PtkA and the two-component-like kinases RsbW and SpoIIAB show the highest propensity to be phosphorylated by other kinases. Analysis of phosphorylated residues on several selected recipient kinases suggests that most cross-phosphorylation events concern key regulatory residues. Therefore, cross-phosphorylation events are very likely to influence the capacity of recipient kinases to phosphorylate substrates downstream in the signal transduction cascade. We therefore conclude that bacterial serine/threonine and tyrosine kinases probably engage in a network-type behavior previously described only in eukaryal cells.http://journal.frontiersin.org/Journal/10.3389/fmicb.2014.00495/fullProtein phosphorylationbacterial protein kinaseprotein kinase cross-talkphosphorylation cascadekinase activation |
| spellingShingle | Lei eShi Nathalie ePigeonneau Vaishnavi eRavikumar Paula eDobrinic Boris eMacek Damjan eFranjevic Marie-Françoise eNoirot-gros Ivan eMijakovic Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues Frontiers in Microbiology Protein phosphorylation bacterial protein kinase protein kinase cross-talk phosphorylation cascade kinase activation |
| title | Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues |
| title_full | Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues |
| title_fullStr | Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues |
| title_full_unstemmed | Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues |
| title_short | Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues |
| title_sort | cross phosphorylation of bacterial serine threonine and tyrosine protein kinases on key regulatory residues |
| topic | Protein phosphorylation bacterial protein kinase protein kinase cross-talk phosphorylation cascade kinase activation |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2014.00495/full |
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