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J Biol Chem, Vol. 275, Issue 2, 729-734, January 14, 2000

Multimeric Self-assembly Equilibria Involving the Histone-like Protein H-NS
A THERMODYNAMIC STUDY*

Simona Ceschini, Giulio Lupidi, Massimo ColettaDagger , Cynthia L. Pon, Evandro Fioretti, and Mauro Angeletti§

From the Department of Molecular, Cellular and Animal Biology, Post-Graduate School in Clinical Biochemistry, University of Camerino, 62032 Camerino (MC) Italy and the Dagger  Department of Experimental Medicine and Biochemical Sciences, University of Roma "Tor Vergata", via di Tor Vergata 135, 00133 Roma, Italy

The thermodynamic parameters affecting protein-protein multimeric self-assembly equilibria of the histone-like protein H-NS were quantified by "large zone" gel-permeation chromatography. The abundance of the different association states (monomer, dimer, and tetramer) were found to be strictly dependent on the monomeric concentration and affected by physical (temperature) and chemical (cations) parameters. On the basis of the results obtained in this study and the available structural information concerning this protein, a mechanism is proposed to explain the association behavior also in relation to the functional properties of the protein.

* This work was supported by grants from the Italian MURST (PRIN "Interazioni proteine-acidi nucleici") and italian C.N.R., and by PF "Biotecnologie" (to C. L. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Tel.: +39-0737-403267; Fax: +39-0737-403351; E-mail: m.angeletti@cambio.unicam.it.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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