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A 6 bp Z‐DNA hairpin binds two Zα domains from the human RNA editing enzyme ADAR1
Author(s) -
Schade Markus,
Behlke Joachim,
Lowenhaupt Ky,
Herbert Alan,
Rich Alexander,
Oschkinat Hartmut
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01119-9
Subject(s) - dna , rna , rna editing , microbiology and biotechnology , dissociation constant , ultracentrifuge , enzyme , chemistry , surface plasmon resonance , z dna , base pair , stereochemistry , biochemistry , biology , gene , receptor , physics , quantum mechanics , nanoparticle
The Zα domain of the human RNA editing enzyme double‐stranded RNA deaminase I (ADAR1) binds to left‐handed Z‐DNA with high affinity. We found by analytical ultracentrifugation and CD spectroscopy that two Zα domains bind to one d(CG) 3 T 4 (CG) 3 hairpin which contains a stem of six base pairs in the Z‐DNA conformation. Both wild‐type Zα and a C125S mutant show a mean dissociation constant of 30 nM as measured by surface plasmon resonance and analytical ultracentrifugation. Our data suggest that short (≥6 bp) segments of Z‐DNA within a gene are able to recruit two ADAR1 enzymes to that particular site.