Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234
The nitrogen-fixing symbiotic bacterium Rhizobium species NGR234 secretes, via a type III secretion system (TTSS), proteins called Nops (nodulation outer proteins). Abolition of TTSS-dependent protein secretion has either no effect or leads to a change in the number of nodules on selected plants. Mo...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
The American Phytopathological Society
2003-09-01
|
| Series: | Molecular Plant-Microbe Interactions |
| Subjects: | |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.9.743 |
| _version_ | 1811290334207934464 |
|---|---|
| author | Corinne Marie William J. Deakin Virginie Viprey Joanna Kopciñska Wladyslaw Golinowski Hari B. Krishnan Xavier Perret William J. Broughton |
| author_facet | Corinne Marie William J. Deakin Virginie Viprey Joanna Kopciñska Wladyslaw Golinowski Hari B. Krishnan Xavier Perret William J. Broughton |
| author_sort | Corinne Marie |
| collection | DOAJ |
| description | The nitrogen-fixing symbiotic bacterium Rhizobium species NGR234 secretes, via a type III secretion system (TTSS), proteins called Nops (nodulation outer proteins). Abolition of TTSS-dependent protein secretion has either no effect or leads to a change in the number of nodules on selected plants. More dramatically, Nops impair nodule development on Crotalaria juncea roots, resulting in the formation of nonfixing pseudonodules. A double mutation of nopX and nopL, which code for two previously identified secreted proteins, leads to a phenotype on Pachyrhizus tuberosus differing from that of a mutant in which the TTSS is not functional. Use of antibodies and a modification of the purification protocol revealed that NGR234 secretes additional proteins in a TTSS-dependent manner. One of them was identified as NopA, a small 7-kDa protein. Single mutations in nopX and nopL were also generated to assess the involvement of each Nop in protein secretion and nodule formation. Mutation of nopX had little effect on NopL and NopA secretion but greatly affected the interaction of NGR234 with many plant hosts tested. NopL was not necessary for the secretion of any Nops but was required for efficient nodulation of some plant species. NopL may thus act as an effector protein whose recognition is dependent upon the hosts' genetic background. |
| first_indexed | 2024-04-13T04:09:47Z |
| format | Article |
| id | doaj.art-67307ca83aab4064bc2d93bc215edd99 |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-04-13T04:09:47Z |
| publishDate | 2003-09-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-67307ca83aab4064bc2d93bc215edd992022-12-22T03:03:07ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062003-09-0116974375110.1094/MPMI.2003.16.9.743Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234Corinne MarieWilliam J. DeakinVirginie VipreyJoanna KopciñskaWladyslaw GolinowskiHari B. KrishnanXavier PerretWilliam J. BroughtonThe nitrogen-fixing symbiotic bacterium Rhizobium species NGR234 secretes, via a type III secretion system (TTSS), proteins called Nops (nodulation outer proteins). Abolition of TTSS-dependent protein secretion has either no effect or leads to a change in the number of nodules on selected plants. More dramatically, Nops impair nodule development on Crotalaria juncea roots, resulting in the formation of nonfixing pseudonodules. A double mutation of nopX and nopL, which code for two previously identified secreted proteins, leads to a phenotype on Pachyrhizus tuberosus differing from that of a mutant in which the TTSS is not functional. Use of antibodies and a modification of the purification protocol revealed that NGR234 secretes additional proteins in a TTSS-dependent manner. One of them was identified as NopA, a small 7-kDa protein. Single mutations in nopX and nopL were also generated to assess the involvement of each Nop in protein secretion and nodule formation. Mutation of nopX had little effect on NopL and NopA secretion but greatly affected the interaction of NGR234 with many plant hosts tested. NopL was not necessary for the secretion of any Nops but was required for efficient nodulation of some plant species. NopL may thus act as an effector protein whose recognition is dependent upon the hosts' genetic background.https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.9.743legumespathogenicitysymbiosistranslocator |
| spellingShingle | Corinne Marie William J. Deakin Virginie Viprey Joanna Kopciñska Wladyslaw Golinowski Hari B. Krishnan Xavier Perret William J. Broughton Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234 Molecular Plant-Microbe Interactions legumes pathogenicity symbiosis translocator |
| title | Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234 |
| title_full | Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234 |
| title_fullStr | Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234 |
| title_full_unstemmed | Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234 |
| title_short | Characterization of Nops, Nodulation Outer Proteins, Secreted Via the Type III Secretion System of NGR234 |
| title_sort | characterization of nops nodulation outer proteins secreted via the type iii secretion system of ngr234 |
| topic | legumes pathogenicity symbiosis translocator |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.9.743 |
| work_keys_str_mv | AT corinnemarie characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT williamjdeakin characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT virginieviprey characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT joannakopcinska characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT wladyslawgolinowski characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT haribkrishnan characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT xavierperret characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 AT williamjbroughton characterizationofnopsnodulationouterproteinssecretedviathetypeiiisecretionsystemofngr234 |