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Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes
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| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , , , |
| In: | Journal of Bacteriology, 193, 2011, 13, S. 3246-3256 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Plocinski, P. Ziolkiewicz, M. Kiran, M. Vadrevu, S. I. Nguyen, H. B. Hugonnet, J. Veckerle, C. Arthur, M. Dziadek, J. Cross, T. A. Madiraju, M. Rajagopalan, M. Plocinski, P. Ziolkiewicz, M. Kiran, M. Vadrevu, S. I. Nguyen, H. B. Hugonnet, J. Veckerle, C. Arthur, M. Dziadek, J. Cross, T. A. Madiraju, M. Rajagopalan, M. |
|---|---|
| author |
Plocinski, P. Ziolkiewicz, M. Kiran, M. Vadrevu, S. I. Nguyen, H. B. Hugonnet, J. Veckerle, C. Arthur, M. Dziadek, J. Cross, T. A. Madiraju, M. Rajagopalan, M. |
| spellingShingle |
Plocinski, P. Ziolkiewicz, M. Kiran, M. Vadrevu, S. I. Nguyen, H. B. Hugonnet, J. Veckerle, C. Arthur, M. Dziadek, J. Cross, T. A. Madiraju, M. Rajagopalan, M. Journal of Bacteriology Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes Molecular Biology Microbiology |
| author_sort |
plocinski, p. |
| spelling |
Plocinski, P. Ziolkiewicz, M. Kiran, M. Vadrevu, S. I. Nguyen, H. B. Hugonnet, J. Veckerle, C. Arthur, M. Dziadek, J. Cross, T. A. Madiraju, M. Rajagopalan, M. 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00188-11 <jats:title>ABSTRACT</jats:title> <jats:p> The role(s) in cell division of the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium tuberculosis</jats:named-content> Rv0011c gene product, a homolog of the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Streptomyces</jats:named-content> CrgA protein that is responsible for coordinating growth and cytokinesis in sporogenic aerial hyphae, is largely unknown. We show that an enhanced cyan fluorescent protein- <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> CrgA (ECFP-CrgA <jats:sub>MT</jats:sub> ) fusion protein is localized to the cell membrane, midcell, and cell pole regions in <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium smegmatis</jats:named-content> . Furthermore, the ECFP-CrgA <jats:sub>MT</jats:sub> fusion protein colocalized with FtsZ-enhanced yellow fluorescent protein (EYFP) in <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content> . Bacterial two-hybrid assays indicated strong interactions of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> CrgA with FtsZ, FtsQ, and the class B penicillin-binding proteins, FtsI (PBPB) and PBPA. The midcell localization of CrgA <jats:sub>MT</jats:sub> was severely compromised under conditions of FtsZ depletion, which indicated that CrgA localizes to the midcell region after assembly of the FtsZ ring. <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> cells with reduced CrgA levels were elongated and grew more slowly than wild-type cells, which indicated defects in cell division, whereas CrgA overproduction did not show growth defects. A <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content> Δ <jats:italic>crgA</jats:italic> strain exhibited a bulged cell morphology, elongated cells with a chain-like phenotype, cells with polar bulbous structures, and a modest growth defect. FtsZ and FtsI levels were not affected in cells producing altered levels of CrgA. Septal and membrane localization of GFP-FtsI was enhanced by CrgA overproduction and was diminished in a Δ <jats:italic>crgA</jats:italic> strain, which indicates that one role of CrgA is to promote and/or stabilize FtsI localization. Overall, these data indicate that CrgA is a novel member of the cell division complex in mycobacteria and possibly facilitates septum formation. </jats:p> Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes Journal of Bacteriology |
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American Society for Microbiology, 2011 |
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American Society for Microbiology, 2011 |
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2011 |
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American Society for Microbiology |
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ai |
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ai |
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Journal of Bacteriology |
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49 |
| title |
Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_unstemmed |
Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_full |
Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_fullStr |
Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_full_unstemmed |
Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_short |
Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_sort |
characterization of crga, a new partner of the mycobacterium tuberculosis peptidoglycan polymerization complexes |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.00188-11 |
| publishDate |
2011 |
| physical |
3246-3256 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
The role(s) in cell division of the
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium tuberculosis</jats:named-content>
Rv0011c gene product, a homolog of the
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Streptomyces</jats:named-content>
CrgA protein that is responsible for coordinating growth and cytokinesis in sporogenic aerial hyphae, is largely unknown. We show that an enhanced cyan fluorescent protein-
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content>
CrgA (ECFP-CrgA
<jats:sub>MT</jats:sub>
) fusion protein is localized to the cell membrane, midcell, and cell pole regions in
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium smegmatis</jats:named-content>
. Furthermore, the ECFP-CrgA
<jats:sub>MT</jats:sub>
fusion protein colocalized with FtsZ-enhanced yellow fluorescent protein (EYFP) in
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content>
. Bacterial two-hybrid assays indicated strong interactions of
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content>
CrgA with FtsZ, FtsQ, and the class B penicillin-binding proteins, FtsI (PBPB) and PBPA. The midcell localization of CrgA
<jats:sub>MT</jats:sub>
was severely compromised under conditions of FtsZ depletion, which indicated that CrgA localizes to the midcell region after assembly of the FtsZ ring.
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content>
cells with reduced CrgA levels were elongated and grew more slowly than wild-type cells, which indicated defects in cell division, whereas CrgA overproduction did not show growth defects. A
<jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content>
Δ
<jats:italic>crgA</jats:italic>
strain exhibited a bulged cell morphology, elongated cells with a chain-like phenotype, cells with polar bulbous structures, and a modest growth defect. FtsZ and FtsI levels were not affected in cells producing altered levels of CrgA. Septal and membrane localization of GFP-FtsI was enhanced by CrgA overproduction and was diminished in a Δ
<jats:italic>crgA</jats:italic>
strain, which indicates that one role of CrgA is to promote and/or stabilize FtsI localization. Overall, these data indicate that CrgA is a novel member of the cell division complex in mycobacteria and possibly facilitates septum formation.
</jats:p> |
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| author | Plocinski, P., Ziolkiewicz, M., Kiran, M., Vadrevu, S. I., Nguyen, H. B., Hugonnet, J., Veckerle, C., Arthur, M., Dziadek, J., Cross, T. A., Madiraju, M., Rajagopalan, M. |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> The role(s) in cell division of the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium tuberculosis</jats:named-content> Rv0011c gene product, a homolog of the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Streptomyces</jats:named-content> CrgA protein that is responsible for coordinating growth and cytokinesis in sporogenic aerial hyphae, is largely unknown. We show that an enhanced cyan fluorescent protein- <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> CrgA (ECFP-CrgA <jats:sub>MT</jats:sub> ) fusion protein is localized to the cell membrane, midcell, and cell pole regions in <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium smegmatis</jats:named-content> . Furthermore, the ECFP-CrgA <jats:sub>MT</jats:sub> fusion protein colocalized with FtsZ-enhanced yellow fluorescent protein (EYFP) in <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content> . Bacterial two-hybrid assays indicated strong interactions of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> CrgA with FtsZ, FtsQ, and the class B penicillin-binding proteins, FtsI (PBPB) and PBPA. The midcell localization of CrgA <jats:sub>MT</jats:sub> was severely compromised under conditions of FtsZ depletion, which indicated that CrgA localizes to the midcell region after assembly of the FtsZ ring. <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> cells with reduced CrgA levels were elongated and grew more slowly than wild-type cells, which indicated defects in cell division, whereas CrgA overproduction did not show growth defects. A <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content> Δ <jats:italic>crgA</jats:italic> strain exhibited a bulged cell morphology, elongated cells with a chain-like phenotype, cells with polar bulbous structures, and a modest growth defect. FtsZ and FtsI levels were not affected in cells producing altered levels of CrgA. Septal and membrane localization of GFP-FtsI was enhanced by CrgA overproduction and was diminished in a Δ <jats:italic>crgA</jats:italic> strain, which indicates that one role of CrgA is to promote and/or stabilize FtsI localization. Overall, these data indicate that CrgA is a novel member of the cell division complex in mycobacteria and possibly facilitates septum formation. </jats:p> |
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| spelling | Plocinski, P. Ziolkiewicz, M. Kiran, M. Vadrevu, S. I. Nguyen, H. B. Hugonnet, J. Veckerle, C. Arthur, M. Dziadek, J. Cross, T. A. Madiraju, M. Rajagopalan, M. 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00188-11 <jats:title>ABSTRACT</jats:title> <jats:p> The role(s) in cell division of the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium tuberculosis</jats:named-content> Rv0011c gene product, a homolog of the <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Streptomyces</jats:named-content> CrgA protein that is responsible for coordinating growth and cytokinesis in sporogenic aerial hyphae, is largely unknown. We show that an enhanced cyan fluorescent protein- <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> CrgA (ECFP-CrgA <jats:sub>MT</jats:sub> ) fusion protein is localized to the cell membrane, midcell, and cell pole regions in <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Mycobacterium smegmatis</jats:named-content> . Furthermore, the ECFP-CrgA <jats:sub>MT</jats:sub> fusion protein colocalized with FtsZ-enhanced yellow fluorescent protein (EYFP) in <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content> . Bacterial two-hybrid assays indicated strong interactions of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> CrgA with FtsZ, FtsQ, and the class B penicillin-binding proteins, FtsI (PBPB) and PBPA. The midcell localization of CrgA <jats:sub>MT</jats:sub> was severely compromised under conditions of FtsZ depletion, which indicated that CrgA localizes to the midcell region after assembly of the FtsZ ring. <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. tuberculosis</jats:named-content> cells with reduced CrgA levels were elongated and grew more slowly than wild-type cells, which indicated defects in cell division, whereas CrgA overproduction did not show growth defects. A <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">M. smegmatis</jats:named-content> Δ <jats:italic>crgA</jats:italic> strain exhibited a bulged cell morphology, elongated cells with a chain-like phenotype, cells with polar bulbous structures, and a modest growth defect. FtsZ and FtsI levels were not affected in cells producing altered levels of CrgA. Septal and membrane localization of GFP-FtsI was enhanced by CrgA overproduction and was diminished in a Δ <jats:italic>crgA</jats:italic> strain, which indicates that one role of CrgA is to promote and/or stabilize FtsI localization. Overall, these data indicate that CrgA is a novel member of the cell division complex in mycobacteria and possibly facilitates septum formation. </jats:p> Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes Journal of Bacteriology |
| spellingShingle | Plocinski, P., Ziolkiewicz, M., Kiran, M., Vadrevu, S. I., Nguyen, H. B., Hugonnet, J., Veckerle, C., Arthur, M., Dziadek, J., Cross, T. A., Madiraju, M., Rajagopalan, M., Journal of Bacteriology, Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes, Molecular Biology, Microbiology |
| title | Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_full | Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_fullStr | Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_full_unstemmed | Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_short | Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| title_sort | characterization of crga, a new partner of the mycobacterium tuberculosis peptidoglycan polymerization complexes |
| title_unstemmed | Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.00188-11 |