A 6 bp Z‐DNA hairpin binds two Zα domains from the human RNA editing enzyme ADAR1

FEBS Letters

Rich, Alexander³  Herbert, Alan³  Behlke, Joachim¹  Oschkinat, Hartmut²  Lowenhaupt, Ky³  Schade, Markus³ 

[1] Max Delbrück Center for Molecular Medicine, 13122 Berlin, Germany;Forschungsinstitut für molekulare Pharmakologie, Alfred-Kowalke-Str. 4, 10315 Berlin, Germany;Department of Biology, Massachusetts Institute of Technology (MIT), 77 Mass. Av., Cambridge, MA 02139, USA

关键词: RNA editing;    ADAR1;    Zα;    Z-DNA;    Helix-turn-helix;    Ultracentrifugation;    ADAR1;    adenosine deaminase dsRNA specific 1;    AMPA;    α-amino-3-hydroxy-5-methyl-4-isoxaleproprionate;    CD;    circular dichroism;    HTH;    helix-turn-helix;    NMR;    nuclear magnetic resonance;   

DOI  :  10.1016/S0014-5793(99)01119-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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)₃T₄(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.

【 授权许可】

Unknown