This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ohashi, T.
Right arrow Articles by Erickson, H. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohashi, T.
Right arrow Articles by Erickson, H. P.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2002, p. 4313-4315, Vol. 184, No. 15
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.15.4313-4315.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Structural Evidence that the P/Q Domain of ZipA Is an Unstructured, Flexible Tether between the Membrane and the C-Terminal FtsZ-Binding Domain

Tomoo Ohashi,1 Cynthia A. Hale,2 Piet A. J. de Boer,2 and Harold P. Erickson1*

Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710-3709,1 Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-49602

Received 27 February 2002/ Accepted 6 May 2002

The cell division protein ZipA has an N-terminal transmembrane domain and a C-terminal globular domain that binds FtsZ. Between them are a charged domain and a P/Q domain rich in proline and glutamine that has been proposed to be an unfolded polypeptide. Here we provide evidence obtained by electron microscopy that the P/Q domain is a flexible tether ranging in length from 8 to 20 nm and invisible in rotary shadowing electron microscopy. We estimated a persistence length of 0.66 nm, which is similar to the persistence lengths of other unfolded and unstructured polypeptides.

* Corresponding author. Mailing address: Department of Cell Biology, Duke University Medical Center, Durham, NC 27710-3709. Phone: (919) 684-6385. Fax: (919) 681-7978. E-mail: H.Erickson{at}cellbio.Duke.edu.

Journal of Bacteriology, August 2002, p. 4313-4315, Vol. 184, No. 15
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.15.4313-4315.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hett, E. C., Rubin, E. J. (2008). Bacterial Growth and Cell Division: a Mycobacterial Perspective. Microbiol. Mol. Biol. Rev. 72: 126-156 [Abstract] [Full Text]  
  • Vicente, M., Rico, A. I., Martinez-Arteaga, R., Mingorance, J. (2006). Septum Enlightenment: Assembly of Bacterial Division Proteins. J. Bacteriol. 188: 19-27 [Full Text]  
  • Johnson, J. E., Lackner, L. L., Hale, C. A., de Boer, P. A. J. (2004). ZipA Is Required for Targeting of DMinC/DicB, but Not DMinC/MinD, Complexes to Septal Ring Assemblies in Escherichia coli. J. Bacteriol. 186: 2418-2429 [Abstract] [Full Text]  
  • Di Lallo, G., Fagioli, M., Barionovi, D., Ghelardini, P., Paolozzi, L. (2003). Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 149: 3353-3359 [Abstract] [Full Text]  
  • Errington, J., Daniel, R. A., Scheffers, D.-J. (2003). Cytokinesis in Bacteria. Microbiol. Mol. Biol. Rev. 67: 52-65 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»