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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 |
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| Personen und Körperschaften: | , , , , , , , , , , , |
| In: | Journal of Bacteriology, 193, 2011, 13, S. 3246-3256 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
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| Schlagwörter: |
| Zusammenfassung: | <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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| Umfang: | 3246-3256 |
| ISSN: |
1098-5530
0021-9193 |
| DOI: | 10.1128/jb.00188-11 |