NDLI: Salt Dependence of IRF1 DBD Binding to DNA Reveals Ions Are Localized Around Protein and DNA

Content Provider	PubMed Central
Author	Hargreaves, Victoria V. Schleif, Robert F.
Abstract	The equilibrium dissociation constant of the DNA binding domain of interferon regulatory factor 1, IRF1 DBD, for its DNA binding site depends strongly on salt concentration and salt type. These dependencies are consistent with IRF1 DBD binding to DNA resulting in cation release from the DNA and both anion release from the protein and cation uptake by the protein. We demonstrated this by utilizing the fact that fluoride's release from protein upon complex formation does not contribute to the salt concentration dependence of binding and by studying mutants in which charged residues in IRF1 DBD that form salt bridges with DNA phosphates are changed to alanine. The salt concentration dependencies of the dissociation constants of wild type IRF1 DBD and the mutants R64A, D73A, K75A, and D73A K75A were measured in buffer containing NaF, NaCl, or NaBr. The salt concentration and type dependencies of the mutants relative to wild type IRF1 DBD provide evidence of charge neutralization by solution ions for R64 and by a salt bridge between D73 and K75 in buffer containing chloride or bromide salts. These data also allowed us to determine the number, type, and localization of condensed ions around both IRF1 DBD and its DNA binding site.
Related Links	http://dx.doi.org/10.1021/bi702082q
Ending Page	4128
Page Count	10
Starting Page	4119
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	13
Volume Number	47
Language	English
Publisher Date	2008-04-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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