title: Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: I. binding to DNA AND to hexon of the precursor to protein VI, pVI, of human adenovirus.
abstract: The precursor to adenovirus protein VI, pVI, is a multifunctional protein with different roles early and late in virus infection. Here, we focus on two roles late in infection, binding of pVI to DNA and to the major capsid protein hexon. pVI bound to DNA as a monomer independent of DNA sequence with an apparent equilibrium dissociation constant, K(d)((app)), of 46 nm. Bound to double-stranded DNA, one molecule of pVI occluded 8 bp. Upon the binding of pVI to DNA, three sodium ions were displaced from the DNA. A ΔG(0)(0) of -4.54 kcal/mol for the nonelectrostatic free energy of binding indicated that a substantial component of the binding free energy resulted from nonspecific interactions between pVI and DNA. The proteolytically processed, mature form of pVI, protein VI, also bound to DNA; its K(d)((app)) was much higher, 307 nm. The binding assays were performed in 1 mm MgCl(2) because in the absence of magnesium, the binding to pVI or protein VI to DNA was too tight to determine a K(d)((app)). Three molecules of pVI bound to one molecule of the hexon trimer with an equilibrium dissociation constant K(d)((app)) of 1.1 nm.
authors.affiliation: Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.
authors.forename: Vito
authors.initials: V
authors.lastname: Graziano
authors.forename: William J
authors.initials: WJ
authors.lastname: McGrath
authors.forename: Maarit
authors.initials: M
authors.lastname: Suomalainen
authors.forename: Urs F
authors.initials: UF
authors.lastname: Greber
authors.forename: Paul
authors.initials: P
authors.lastname: Freimuth
authors.forename: Paul C
authors.initials: PC
authors.lastname: Blainey
authors.forename: Guobin
authors.initials: G
authors.lastname: Luo
authors.forename: X Sunney
authors.initials: XS
authors.lastname: Xie
authors.forename: Walter F
authors.initials: WF
authors.lastname: Mangel
mesh_terms: D000260:Adenoviruses, Human / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry; D036022:Capsid Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002414:Cations, Monovalent; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004279:DNA, Viral / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D015636:Magnesium Chloride / Q000737:chemistry; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012964:Sodium / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D036022:Capsid Proteins; D002414:Cations, Monovalent; D004279:DNA, Viral; D011498:Protein Precursors; D011994:Recombinant Proteins; C018315:hexon capsid protein, Adenovirus; C090876:polypeptide VI, adenovirus; D015636:Magnesium Chloride; D012964:Sodium; D003546:Cysteine Endopeptidases; C091827:adenain