Local conformational changes in the 8–17 deoxyribozyme core induced by activating and inactivating divalent metal ions

Placing 2-aminopurine at position 15 of the 8–17 DNAzyme allows the detection of a specific metal-induced conformational change, apparently coupled to the activation of catalysis.

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Slow Conformational Changes of the Inorganic Pyrophosphatase from Bakers' Yeast Induced by Divalent Metal Ions

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1973.tb02686.x ◽

1973 ◽

Vol 33 (2) ◽

pp. 323-331 ◽

Cited By ~ 15

Author(s):

Wolsfgang E. Hohne ◽

Tom A. Rapoport

Keyword(s):

Metal Ions ◽

Conformational Changes ◽

Divalent Metal ◽

Inorganic Pyrophosphatase ◽

Divalent Metal Ions

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Divalent metal ions induce conformational change in pure, human wild-type p53 tumor suppressor protein

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(94)90197-x ◽

1994 ◽

Vol 1209 (2) ◽

pp. 279-285 ◽

Cited By ~ 15

Author(s):

Arnold I. Coffer ◽

Phillip P. Knowles

Keyword(s):

Tumor Suppressor ◽

Metal Ions ◽

Conformational Change ◽

Divalent Metal ◽

Tumor Suppressor Protein ◽

Wild Type ◽

Divalent Metal Ions ◽

P53 Tumor Suppressor ◽

P53 Tumor Suppressor Protein ◽

Human Wild Type

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pH-Dependent amino acid induced conformational changes of rabbit muscle pyruvate kinase

Canadian Journal of Biochemistry ◽

10.1139/o80-025 ◽

1980 ◽

Vol 58 (3) ◽

pp. 188-193 ◽

Cited By ~ 9

Author(s):

Chiu-Yin Kwan ◽

Robert C. Davis

Keyword(s):

Metal Ions ◽

Pyruvate Kinase ◽

Conformational Changes ◽

Divalent Metal ◽

Rabbit Muscle ◽

Divalent Metal Ions ◽

Spectral Changes ◽

Metal Derivatives ◽

Muscle Pyruvate Kinase ◽

Difference Absorption

The interactions of L-Phe and L-Ala with rabbit muscle pyruvate kinase depended upon the nature of divalent metal ions studied: Mg(II), Co(II), Mn(II), and Ni(II). L-Phe inhibited all metal derivatives of the enzyme except Mn(II)–enzyme. L-Ala inhibited only Ni(II)–enzyme and had no effect on other metal derivatives. The inhibition by L-Phe could be partially or completely reversed by L-Ala for all metal derivatives. The mode of inhibition of pyruvate kinase by L-Phe depended upon pH as well as the nature of activating divalent metal ions. The sigmoidal response increased with increasing pH for all metal derivatives inhibited by L-Phe. L-Phe and L-Ala strongly perturbed the coordination sphere of enzyme bound Co(II), but not Ni(II). There were poor correlations between visible circular dichroic (cd) spectral changes and the corresponding kinetic changes. However, L-Phe and (or) L-Ala induced ultraviolet cd and difference absorption spectral changes, on the other hand, corresponded remarkably well with the kinetic observations.

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A cooperative conformational change in duplex DNA induced by Zn2+ and other divalent metal ions

Biochemistry and Cell Biology ◽

10.1139/o93-026 ◽

1993 ◽

Vol 71 (3-4) ◽

pp. 162-168 ◽

Cited By ~ 130

Author(s):

Jeremy S. Lee ◽

Laura J. P. Latimer ◽

R. Stephen Reid

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Metal Ions ◽

Conformational Change ◽

Divalent Metal ◽

Proton Nuclear Magnetic Resonance ◽

Duplex Dna ◽

Divalent Metal Ions ◽

Base Pairs ◽

Nuclear Magnetic

Zn2+ and some other divalent metal ions bind to duplex DNA at pHs above 8 and cause a conformational change. This new structure does not bind ethidium, allowing the development of a rapid fluorescence assay. All duplex DNAs, regardless of sequence or G∙C content, can form this structure. The rate of formation shows a strong dependence on temperature, pH, and Zn2+ concentration; at 20 °C, 1 mM Zn2+, and pH 8.6 the dismutation is half complete in 30 min. Addition of EDTA causes rapid reversion to 'B' DNA, showing that the new conformation retains two strands that are antiparallel. Unlike the ultraviolet or circular dichroism spectra, the nuclear magnetic resonance spectrum was informative since the imino protons of both A∙T and G∙C base pairs are lost upon addition of a stoichiometric amount of Zn2+. The pitch of the helix was estimated from gel electrophoresis of circular DNAs in the presence of Zn2+ and it contains at least 5% fewer base pairs per turn than 'B' DNA. The transformation is cooperative and shows hysteresis, suggesting that this is a distinct structure and not simply a minor variant of 'B' DNA. It is proposed to call this new structure 'M' DNA because of the intimate involvement of metal ions.Key words: DNA conformation, cooperative transition, ethidium binding, divalent metal ions, proton nuclear magnetic resonance.

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