Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity
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<sup>+</sup>. In this study, we investigated the conformational heterogeneity of a G-rich seq...
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MDPI AG
2019-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/24/10/1988 |
| _version_ | 1818336380958277632 |
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| author | Mykhailo Kopylov Trevia M. Jackson M. Elizabeth Stroupe |
| author_facet | Mykhailo Kopylov Trevia M. Jackson M. Elizabeth Stroupe |
| author_sort | Mykhailo Kopylov |
| collection | DOAJ |
| description | 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<sup>+</sup>. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i>Zea mays</i> <i>hexokinase4</i> 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. |
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| format | Article |
| id | doaj.art-13f49b98340644a1a25e77855b205070 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-13T14:38:25Z |
| publishDate | 2019-05-01 |
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| series | Molecules |
| spelling | doaj.art-13f49b98340644a1a25e77855b2050702022-12-21T23:41:40ZengMDPI AGMolecules1420-30492019-05-012410198810.3390/molecules24101988molecules24101988Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding SpecificityMykhailo Kopylov0Trevia M. Jackson1M. Elizabeth Stroupe2Department of Biological Science and Institute of Molecular Biophysics, Florida State University, 91 Chieftain Way, Tallahassee, FL 32306, USADepartment of Biological Science and Institute of Molecular Biophysics, Florida State University, 91 Chieftain Way, Tallahassee, FL 32306, USADepartment of Biological Science and Institute of Molecular Biophysics, Florida State University, 91 Chieftain Way, Tallahassee, FL 32306, USAGuanine-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<sup>+</sup>. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i>Zea mays</i> <i>hexokinase4</i> 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.https://www.mdpi.com/1420-3049/24/10/1988G-quadruplexG4nucleoside diphosphate kinaseNDPK |
| spellingShingle | Mykhailo Kopylov Trevia M. Jackson M. Elizabeth Stroupe Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity Molecules G-quadruplex G4 nucleoside diphosphate kinase NDPK |
| title | Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity |
| title_full | Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity |
| title_fullStr | Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity |
| title_full_unstemmed | Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity |
| title_short | Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity |
| title_sort | bulged and canonical g quadruplex conformations determine ndpk binding specificity |
| topic | G-quadruplex G4 nucleoside diphosphate kinase NDPK |
| url | https://www.mdpi.com/1420-3049/24/10/1988 |
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