Apparent cooperative assembly of the bacterial cell division protein FtsZ demonstrated by isothermal titration calorimetry

Michael Caplan, Harold P. Erickson

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The assembly dynamics of FtsZ, a prokaryotic homolog of tubulin, are important for their role in bacterial cytokinesis. Here we used isothermal titration calorimetry (ITC) to measure the heat of FtsZ self-association under various conditions. The measurements were designed to test whether FtsZ protofilaments are assembled by an isodesmic (linear aggregates in which each bond has an identical equilibrium constant) or a cooperative (aggregates only become stable after forming a oligomeric nucleus) assembly process. The isodesmic model can fit the assembly in GDP closely but cannot fit the assembly in GTP. FtsZ-GTP without Mg2+ exhibits an apparent critical concentration, which is indicative of cooperative assembly, near 2.9 μM. With 2.5 mM Mg2+ (which allows FtsZ to hydrolyze GTP) the critical concentration is reduced 10-fold to ∼0.31 μM. Both with and without Mg2+ there is no evidence for assembly below the critical concentration, but there is an abrupt transition to full assembly above. The ITC data are highly suggestive of a cooperative assembly, although this is difficult to reconcile with the 1-subunit-thick protofilaments observed by electron microscopy.

Original languageEnglish (US)
Pages (from-to)13784-13788
Number of pages5
JournalJournal of Biological Chemistry
Volume278
Issue number16
DOIs
StatePublished - Apr 18 2003

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Calorimetry
Guanosine Triphosphate
Titration
Cell Division
Cells
Proteins
Cytokinesis
Tubulin
Electron Microscopy
Hot Temperature
Equilibrium constants
Electron microscopy
Association reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Apparent cooperative assembly of the bacterial cell division protein FtsZ demonstrated by isothermal titration calorimetry. / Caplan, Michael; Erickson, Harold P.

In: Journal of Biological Chemistry, Vol. 278, No. 16, 18.04.2003, p. 13784-13788.

Research output: Contribution to journalArticle

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