M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog.
Receptor Ser/Thr protein kinases are candidates for sensors that govern developmental changes and disease processes of Mycobacterium tuberculosis (Mtb), but the functions of these kinases are not established. Here, we show that Mtb protein kinase (Pkn) D overexpression alters transcription of numero...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2007-04-01
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| Series: | PLoS Pathogens |
| Online Access: | http://europepmc.org/articles/PMC1847690?pdf=render |
| _version_ | 1811218173699031040 |
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| author | Andrew E Greenstein Jason A MacGurn Christina E Baer Arnold M Falick Jeffery S Cox Tom Alber |
| author_facet | Andrew E Greenstein Jason A MacGurn Christina E Baer Arnold M Falick Jeffery S Cox Tom Alber |
| author_sort | Andrew E Greenstein |
| collection | DOAJ |
| description | Receptor Ser/Thr protein kinases are candidates for sensors that govern developmental changes and disease processes of Mycobacterium tuberculosis (Mtb), but the functions of these kinases are not established. Here, we show that Mtb protein kinase (Pkn) D overexpression alters transcription of numerous bacterial genes, including Rv0516c, a putative anti-anti-sigma factor, and genes regulated by sigma factor F. The PknD kinase domain directly phosphorylated Rv0516c, but no other sigma factor regulator, in vitro. In contrast, the purified PknB and PknE kinase domains phosphorylated distinct sigma regulators. Rather than modifying a consensus site, PknD phosphorylated Rv0516c in vitro and in vivo on Thr2 in a unique N-terminal extension. This phosphorylation inhibited Rv0516c binding in vitro to a homologous anti-anti-sigma factor, Rv2638. These results support a model in which signals transmitted through PknD alter the transcriptional program of Mtb by stimulating phosphorylation of a sigma factor regulator at an unprecedented control site. |
| first_indexed | 2024-04-12T07:05:06Z |
| format | Article |
| id | doaj.art-9bd8349551f84deeb318054388395c9b |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-04-12T07:05:06Z |
| publishDate | 2007-04-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-9bd8349551f84deeb318054388395c9b2022-12-22T03:42:50ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742007-04-0134e4910.1371/journal.ppat.0030049M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog.Andrew E GreensteinJason A MacGurnChristina E BaerArnold M FalickJeffery S CoxTom AlberReceptor Ser/Thr protein kinases are candidates for sensors that govern developmental changes and disease processes of Mycobacterium tuberculosis (Mtb), but the functions of these kinases are not established. Here, we show that Mtb protein kinase (Pkn) D overexpression alters transcription of numerous bacterial genes, including Rv0516c, a putative anti-anti-sigma factor, and genes regulated by sigma factor F. The PknD kinase domain directly phosphorylated Rv0516c, but no other sigma factor regulator, in vitro. In contrast, the purified PknB and PknE kinase domains phosphorylated distinct sigma regulators. Rather than modifying a consensus site, PknD phosphorylated Rv0516c in vitro and in vivo on Thr2 in a unique N-terminal extension. This phosphorylation inhibited Rv0516c binding in vitro to a homologous anti-anti-sigma factor, Rv2638. These results support a model in which signals transmitted through PknD alter the transcriptional program of Mtb by stimulating phosphorylation of a sigma factor regulator at an unprecedented control site.http://europepmc.org/articles/PMC1847690?pdf=render |
| spellingShingle | Andrew E Greenstein Jason A MacGurn Christina E Baer Arnold M Falick Jeffery S Cox Tom Alber M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. PLoS Pathogens |
| title | M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. |
| title_full | M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. |
| title_fullStr | M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. |
| title_full_unstemmed | M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. |
| title_short | M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. |
| title_sort | m tuberculosis ser thr protein kinase d phosphorylates an anti anti sigma factor homolog |
| url | http://europepmc.org/articles/PMC1847690?pdf=render |
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