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J. Biol. Chem., Vol. 275, Issue 44, 34826-34832, November 3, 2000

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Attractive Interhelical Electrostatic Interactions in the Proline- and Acidic-rich Region (PAR) Leucine Zipper Subfamily Preclude Heterodimerization with Other Basic Leucine Zipper Subfamilies^*

Jonathan R. Moll, Michelle Olive^§, and Charles Vinson^¶

From the  Laboratory of Metabolism, NCI, National Institutes of Health, Bethesda, Maryland 20892 and ^§  Unite 441, INSERM, 33600 Pessac, France

Basic region-leucine zipper (B-ZIP) proteins homo- or heterodimerize to bind sequence-specific double-stranded DNA. We present circular dichroism (CD) thermal denaturation data on vitellogenin promoter-binding protein (VBP), a member of the PAR subfamily of B-ZIP proteins that also includes thyroid embryonic factor, hepatocyte leukemia factor, and albumin site D-binding protein. VBP does not heterodimerize with B-ZIP domains from C/EBP, JUND, or FOS. We describe a dominant negative protein, A-VBP, that contains the VBP leucine zipper and an acidic amphipathic protein sequence that replaces the basic region critical for DNA binding. The acidic extension forms a coiled coil structure with the VBP basic region in the VBP·A-VBP heterodimer. This new -helical structure extends the leucine zipper N-terminally, stabilizing the complex by 2.0 kcal/mol. A-VBP abolishes DNA binding of VBP in an equimolar competition assay, but does not affect DNA binding even at 100-fold excess of CREB, C/EBP, or FOS/JUND. Likewise, proteins containing the acidic extension appended to seven other leucine zippers do not inhibit VBP DNA binding. We show that conserved g  e' or i, i' +5 salt bridges are sufficient to confer specificity to VBP by mutating the C/EBP leucine zipper to contain the g  e' salt bridges that characterize VBP. A-VBP heterodimerizes with this mutant C/EBP, preventing it from binding to DNA. These conserved g  e' electrostatic interactions define the specificity of the PAR subfamily of B-ZIP proteins and preclude interaction with other B-ZIP subfamilies.

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