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Journal of Bacteriology, July 2004, p. 4254-4261, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4254-4261.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Energetics of Gliding Motility in Mycoplasma mobile

Jacob D. Jaffe,1,2 Makoto Miyata,3,4 and Howard C. Berg1,5*

Department of Molecular and Cellular Biology, Harvard University, Cambridge,1 Department of Genetics, Harvard Medical School, Boston, Massachusetts,2 Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku,3 PRESTO, Japan Science and Technology Corporation, Osaka 558-8585, Japan,4 The Rowland Institute at Harvard, Cambridge, Massachusetts5

Received 31 December 2003/ Accepted 18 February 2004

Mycoplasma mobile glides on surfaces at up to 7 µm/s by an unknown mechanism. We studied the energetics that power gliding by using a novel, growth medium-free system. We found that cells could glide in defined media if the glass substrate is preconditioned by exposure to horse serum. The active component that potentiates gliding is sensitive to proteinase K treatment. We used the defined medium system to test the effect of various inhibitors, ionophores, and poisons on motility of M. mobile. Valinomycin, carbonyl cyanide 4-(trifluoromethoxy)phenylhydrazone (FCCP), N,N'-dicyclohexylcarbodiimide, phenamil, amiloride, rifampin, and puromycin had no short-term effects on gliding. We also confirmed that we were able to modulate the membrane potential with valinomycin and FCCP by using a potential-sensitive dye. Shifting the pH likewise had no effect on motility. These results rule out the use of conventional ion motive forces to power gliding. Arsenate had a dramatic inhibitory effect on gliding, and both the speed and the fraction of cells moving tracked ATP levels. Sodium orthovanadate had a slight but significant inhibitory effect on gliding. Taken together, these results suggest that the motor system of M. mobile is likely an ATPase or is directly coupled to an ATPase.

* Corresponding author. Mailing address: 16 Divinity Ave., Biological Laboratories 3063, Cambridge, MA 02138. Phone: (617) 495-0924. Fax: (617) 496-1114. E-mail: hberg{at}mcb.harvard.edu.

Journal of Bacteriology, July 2004, p. 4254-4261, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4254-4261.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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