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Journal of Bacteriology, December 2001, p. 7387-7391, Vol. 183, No. 24
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.24.7387-7891.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Stability and Subcellular Localization of Cytadherence-Associated Protein P65 in Mycoplasma pneumoniae

Jarrat L. Jordan, Karen M. Berry,dagger Mitchell F. Balish, and Duncan C. Krause*

Department of Microbiology, University of Georgia, Athens, Georgia 30602

Received 19 June 2001/Accepted 21 September 2001

The surface protein P65 is a constituent of the Mycoplasma pneumoniae cytoskeleton and is present at reduced levels in mutants lacking the cytadherence accessory protein HMW2. Pulse-chase studies demonstrated that P65 is subject to accelerated turnover in the absence of HMW2. P65 was also less abundant in noncytadhering mutants lacking HMW1 or P30 but was present at wild-type levels in mutants lacking proteins A, B, C, and P1. P65 exhibited a polar localization like that in wild-type M. pneumoniae in all mutants having normal levels of HMW1 and HMW2. Partial or complete loss of these proteins, however, correlated with severe reduction in the P65 level and the inability to localize P65 properly.

* Corresponding author. Mailing address: Department of Microbiology, 523 Biological Sciences Bldg., University of Georgia, Athens, GA 30602. Phone: (706) 542-2671. Fax: (706) 542-2674. E-mail: dkrause{at}arches.uga.edu.

dagger Present address: Foodborne and Diarrheal Diseases Laboratory Section, Centers for Disease Control and Prevention, 1600 Clifton Road, NE, Atlanta, GA 30333.

Journal of Bacteriology, December 2001, p. 7387-7391, Vol. 183, No. 24
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.24.7387-7891.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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