Multimeric self-assembly equilibria involving the histone-like protein H-NS. A thermodynamic study.
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.
Ceschini
S
S
Department of Molecular, Cellular and Animal Biology, Post-Graduate School in Clinical Biochemistry, University of Camerino, 62032 Camerino (MC) Italy.
Lupidi
G
G
Coletta
M
M
Pon
C L
CL
Fioretti
E
E
Angeletti
M
M
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002151:Calorimetry; D002414:Cations, Monovalent / Q000494:pharmacology; D002850:Chromatography, Gel; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013816:Thermodynamics
D001426:Bacterial Proteins; D002414:Cations, Monovalent; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria; D046911:Macromolecular Substances; D011994:Recombinant Proteins