Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M301303200 on March 20, 2003

J. Biol. Chem., Vol. 278, Issue 24, 21336-21343, June 13, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/24/21336    most recent
M301303200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Santra, M. K.
Right arrow Articles by Panda, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Santra, M. K.
Right arrow Articles by Panda, D.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Detection of an Intermediate during Unfolding of Bacterial Cell Division Protein FtsZ

LOSS OF FUNCTIONAL PROPERTIES PRECEDES THE GLOBAL UNFOLDING OF FtsZ*

Manas K. Santra {ddagger} and Dulal Panda §

From the School of Biosciences and Bioengineering, Indian Institute of Technology, Bombay, Powai, Mumbai 400 076, India

Using environment-sensitive fluorescence of 1-anilinonaphthalene-8-sulfonic acid, polarization of fluorescein 5'-isothiocyanate-labeled FtsZ, and far-UV circular dichroism spectroscopy, the chemical unfolding of FtsZ was found to proceed through two steps. The first step of the urea-induced unfolding produced an intermediate, which then unfolded at higher concentrations of urea. The intermediate state contains native-like secondary structure and much less tertiary structure compared with the native state. It is distinct from the native state as well as from the unfolded state. Similar to urea-induced unfolding of FtsZ, thermal unfolding of FtsZ also occurs in two steps. The midpoints for the first and second thermal unfolding transitions were found to be 38 ± 4 and 77 ± 5 °C, respectively. Further, the functional properties of FtsZ are extremely sensitive to urea, guanidium chloride, and sodium dodecyl sulfate. For example, 50% inhibition of the FtsZ assembly and GTP hydrolysis occurred at 0.1 and 0.2 M of urea, respectively. FtsZ lost its functional properties before any significant perturbation in the secondary or tertiary structure was detected by using several fluorescence techniques and far UV-CD indicating preferential local unfolding of the functional region(s). In addition, the unfolded FtsZ regains its ability to polymerize fully upon removal of urea. The data taken together suggest that FtsZ unfolds reversibly through a multistep process, and local responses that inhibit functional properties precede the global transition of FtsZ to the unfolded state.


Received for publication, February 6, 2003 , and in revised form, March 17, 2003.

* This work was supported by a grant (to D. P.) from the Dept. of Science and Technology, Government of India. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} Supported by a fellowship from the Council of Scientific and Industrial Research, Government of India.

§ To whom correspondence should be addressed. Tel.: 91-22-2572-2545 (ext. 7838); Fax: 91-22-2572-3480; E-mail: panda{at}btc.iitb.ac.in.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. K. Singh, R. D. Makde, V. Kumar, and D. Panda
SepF Increases the Assembly and Bundling of FtsZ Polymers and Stabilizes FtsZ Protofilaments by Binding along Its Length
J. Biol. Chem., November 7, 2008; 283(45): 31116 - 31124.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
K. A. Michie, L. G. Monahan, P. L. Beech, and E. J. Harry
Trapping of a Spiral-Like Intermediate of the Bacterial Cytokinetic Protein FtsZ.
J. Bacteriol., March 1, 2006; 188(5): 1680 - 1690.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
P. Gupta, S. P. Anand, R. Srinivasan, H. Rajeswari, S. Indi, and P. Ajitkumar
The C-terminally truncated MtFtsZ-{Delta}C169 mutant of Mycobacterium tuberculosis FtsZ shows GTPase and GTP-induced, GTP-specific polymerization activities in vitro
Microbiology, December 1, 2004; 150(12): 3906 - 3908.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. K. Santra, T. K. Beuria, A. Banerjee, and D. Panda
Ruthenium Red-induced Bundling of Bacterial Cell Division Protein, FtsZ
J. Biol. Chem., June 18, 2004; 279(25): 25959 - 25965.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement