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Open AccessArticle

Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity

Department of Biological Science and Institute of Molecular Biophysics, Florida State University, 91 Chieftain Way, Tallahassee, FL 32306, USA
New York Structural Biology Center, 89 Convent Ave, New York, NY 10027, USA
Author to whom correspondence should be addressed.
Academic Editor: Sara N. Richter
Molecules 2019, 24(10), 1988;
Received: 23 April 2019 / Revised: 20 May 2019 / Accepted: 22 May 2019 / Published: 23 May 2019
(This article belongs to the Special Issue G-quadruplex and Microorganisms)
Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K+. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the Zea mays hexokinase4 gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s. View Full-Text
Keywords: G-quadruplex; G4; nucleoside diphosphate kinase; NDPK G-quadruplex; G4; nucleoside diphosphate kinase; NDPK
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MDPI and ACS Style

Kopylov, M.; Jackson, T.M.; Stroupe, M.E. Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity. Molecules 2019, 24, 1988.

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