The high salt form of poly(dG-dC)·poly(dG-dC) is left-handed Z-DNA: Raman spectra of crystals and solutions

Z-DNA is stabilized by various Z-DNA binding proteins (ZBPs) that play important roles in RNA editing, innate immune response, and viral infection. In this review, the structural and dynamics of various ZBPs complexed with Z-DNA are summarized to better understand the mechanisms by which ZBPs selectively recognize d(CG)-repeat DNA sequences in genomic DNA and efficiently convert them to left-handed Z-DNA to achieve their biological function. The intermolecular interaction of ZBPs with Z-DNA strands is mediated through a single continuous recognition surface which consists of an α3 helix and a β-hairpin. In the ZBP-Z-DNA complexes, three identical, conserved residues (N173, Y177, and W195 in the Zα domain of human ADAR1) play central roles in the interaction with Z-DNA. ZBPs convert a 6-base DNA pair to a Z-form helix via the B-Z transition mechanism in which the ZBP first binds to B-DNA and then shifts the equilibrium from B-DNA to Z-DNA, a conformation that is then selectively stabilized by the additional binding of a second ZBP molecule. During B-Z transition, ZBPs selectively recognize the alternating d(CG)n sequence and convert it to a Z-form helix in long genomic DNA through multiple sequence discrimination steps. In addition, the intermediate complex formed by ZBPs and B-DNA, which is modulated by varying conditions, determines the degree of B-Z transition.

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Oligonucleotides DNA containing 8-trifluoromethyl-2′-deoxyguanosine for observing Z-DNA structure

Nucleic Acids Research ◽

10.1093/nar/gkaa505 ◽

2020 ◽

Cited By ~ 1

Author(s):

Hong-Liang Bao ◽

Tatsuki Masuzawa ◽

Takanori Oyoshi ◽

Yan Xu

Keyword(s):

Genetic Diseases ◽

Dna Structure ◽

2D Nmr ◽

Living Cells ◽

Molecular Probes ◽

Alternative Form ◽

Left Handed ◽

Z Dna ◽

And Function

Abstract Z-DNA is known to be a left-handed alternative form of DNA and has important biological roles as well as being related to cancer and other genetic diseases. It is therefore important to investigate Z-DNA structure and related biological events in living cells. However, the development of molecular probes for the observation of Z-DNA structures inside living cells has not yet been realized. Here, we have succeeded in developing site-specific trifluoromethyl oligonucleotide DNA by incorporation of 8-trifluoromethyl-2′-deoxyguanosine (FG). 2D NMR strongly suggested that FG adopted a syn conformation. Trifluoromethyl oligonucleotides dramatically stabilized Z-DNA, even under physiological salt concentrations. Furthermore, the trifluoromethyl DNA can be used to directly observe Z-form DNA structure and interaction of DNA with proteins in vitro, as well as in living human cells by19F NMR spectroscopy for the first time. These results provide valuable information to allow understanding of the structure and function of Z-DNA.

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Differential Stabilization of Left-Handed Z-DNA and Z-RNA In Vitro and In Vivo

Enzyme Dynamics and Regulation ◽

10.1007/978-1-4612-3744-0_23 ◽

1988 ◽

pp. 190-199 ◽

Cited By ~ 1

Author(s):

Thomas M. Jovin ◽

Donna J. Arndt-Jovin

Keyword(s):

Left Handed ◽

Z Dna

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Комбинационное рассеяние света в хирально чистых и рацемической фазах поликристаллов триптофана и тирозина

Журнал технической физики ◽

10.21883/os.2019.10.48354.162-19 ◽

2019 ◽

Vol 127 (10) ◽

pp. 541

Author(s):

В.С. Горелик ◽

М.Ф. Умаров ◽

Ю.П. Войнов

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Raman Spectra ◽

Spectral Range ◽

Phase State ◽

Source Parameters ◽

Low Frequency ◽

Aromatic Amino Acids ◽

Chiral Phase ◽

Left Handed

AbstractRaman spectra of tryptophan and tyrosine polycrystals have been analyzed in a wide spectral range by fiber-optic spectroscopy. The Raman spectra have been recorded with a BWS465-785H spectrometer in the spectral range of 0–2700 cm^–1 using a 785-nm cw laser as an excitation source. Parameters of the Raman spectra are compared for three crystalline phase modifications of aromatic amino acids: left-handed, right-handed, and racemic phase. The presence of strong Raman satellites, the characteristics of which change depending on the type of the chiral phase state of amino acid, is found in the low-frequency Raman spectra of tryptophan and tyrosine amino acid lattices. The results obtained can be used for monitoring the chiral purity of bioactive preparations containing amino acids.

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