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Journal of Bacteriology, October 2007, p. 7014-7023, Vol. 189, No. 19
0021-9193/07/$08.00+0     doi:10.1128/JB.00975-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Functional Analysis of the Mycoplasma genitalium MG312 Protein Reveals a Specific Requirement of the MG312 N-Terminal Domain for Gliding Motility{triangledown}

Raul Burgos, Oscar Q. Pich, Enrique Querol, and Jaume Piñol*

Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain

Received 20 June 2007/ Accepted 25 July 2007

The human pathogen Mycoplasma genitalium is known to mediate cell adhesion to target cells by the attachment organelle, a complex structure also implicated in gliding motility. The gliding mechanism of M. genitalium cells is completely unknown, but recent studies have begun to elucidate the components of the gliding machinery. We report the study of MG312, a cytadherence-related protein containing in the N terminus a box enriched in aromatic and glycine residues (EAGR), which is also exclusively found in MG200 and MG386 gliding motility proteins. Characterization of an MG_312 deletion mutant obtained by homologous recombination has revealed that the MG312 protein is required for the assembly of the M. genitalium terminal organelle. This finding is consistent with the intermediate-cytadherence phenotype and the complete absence of gliding motility exhibited by this mutant. Reintroduction of several MG_312 deletion derivatives into the MG_312 null mutant allowed us to identify two separate functional domains: an N-terminal domain implicated in gliding motility and a C-terminal domain involved in cytadherence and terminal organelle assembly functions. In addition, our results also provide evidence that the EAGR box has a specific contribution to mycoplasma cell motion. Finally, the presence of a conserved ATP binding site known as a Walker A box in the MG312 N-terminal region suggests that this structural protein could also play an active function in the gliding mechanism.

* Corresponding author. Mailing address: Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. Phone: 34-93-5811278. Fax: 34-93-5812011. E-mail: jaume.pinyol{at}uab.es

{triangledown} Published ahead of print on 3 August 2007.

Journal of Bacteriology, October 2007, p. 7014-7023, Vol. 189, No. 19
0021-9193/07/$08.00+0     doi:10.1128/JB.00975-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chalker, V. J., Jordan, K., Ali, T., Ison, C. (2009). Real-time PCR detection of the mg219 gene of unknown function of Mycoplasma genitalium in men with and without non-gonococcal urethritis and their female partners in England. J Med Microbiol 58: 895-899 [Abstract] [Full Text]  
  • Pich, O. Q., Burgos, R., Ferrer-Navarro, M., Querol, E., Pinol, J. (2008). Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence. Microbiology 154: 3188-3198 [Abstract] [Full Text]  


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