BIOMAT Database Logo BIOMAT Database Logo

Spectroscopic characterization of a DNA-binding domain, Z alpha, from the editing enzyme, dsRNA adenosine deaminase: evidence for left-handed Z-DNA in the Z alpha-DNA complex. 1998

I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Department of Biology, George R. Harrison Spectroscopy Laboratory, Massachusetts Institute of Technology, Cambridge 02139, USA.

Double-stranded RNA adenosine deaminase (ADAR1) is an ubiquitous enzyme in metazoa that edits pre-mRNA changing adenosine to inosine in regions of double-stranded RNA. Zalpha, an N-terminal domain of human ADAR1 encompassing 76 amino acid residues, shows apparent specificity for the left-handed Z-DNA conformation adopted by alternating (dGdC) polymers modified by bromination or methylation, as well as for (dGdC)13 inserts present in supercoiled plasmids. Here, a combination of circular dichroism, fluorescence, and gel-retardation studies is utilized to characterize recombinant Zalpha peptide and to examine its interaction with DNA. Results from laser-Raman spectroscopy experiments provide direct evidence for the existence of Z-DNA in peptide-DNA complexes.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009690 Nucleic Acid Conformation The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape. DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011089 Polydeoxyribonucleotides A group of 13 or more deoxyribonucleotides in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties. Polydeoxyribonucleotide
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011489 Protein Denaturation Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein. Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D003841 Deoxycytidine A nucleoside component of DNA composed of CYTOSINE and DEOXYRIBOSE. Cytosine Deoxyribonucleoside,Cytosine Deoxyriboside,Deoxyribonucleoside, Cytosine,Deoxyriboside, Cytosine
D003849 Deoxyguanosine A nucleoside consisting of the base guanine and the sugar deoxyribose.

Related Publications

I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
The zalpha domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA.
December 2000, Proceedings of the National Academy of Sciences of the United States of America,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase.
August 1997, Proceedings of the National Academy of Sciences of the United States of America,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1.
April 2007, Structure (London, England : 1993),
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA.
June 1999, Science (New York, N.Y.),
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Evidence for a new Z-type left-handed DNA helix: properties of Z(WC)-DNA.
October 1990, Nucleic acids research,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Crystallization of the Zalpha domain of the human editing enzyme ADAR1 complexed with a DNA-RNA chimeric oligonucleotide in the left-handed Z-conformation.
January 2002, Acta crystallographica. Section D, Biological crystallography,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
[Crystal structure of Z-DNA binding domain bound to left-handed Z-DNA: outstanding achievement of Alexander Rich].
March 2000, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Structure-function analysis of the Z-DNA-binding domain Zalpha of dsRNA adenosine deaminase type I reveals similarity to the (alpha + beta) family of helix-turn-helix proteins.
January 1999, The EMBO journal,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Raman spectroscopic study of left-handed Z-RNA.
December 1987, Biochemistry,
I Berger, and W Winston, and R Manoharan, and T Schwartz, and J Alfken, and Y G Kim, and K Lowenhaupt, and A Herbert, and A Rich
Antibodies specific for left-handed Z-DNA.
June 1981, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!