The double‐stranded RNA‐binding domains of Xenopus laevis ADAR1 exhibit different RNA‐binding behaviors

FEBS Letters

Jantsch, Michael F¹  Brooks, Roman¹  Eckmann, Christian R¹ 

[1] Department of Cytology and Genetics, Institute of Botany, University of Vienna, Rennweg 14, A-1030 Vienna, Austria

关键词: Double-stranded RNA-binding domain;    RNA binding;    RNA editing;    Xenopus laevis;   

DOI  :  10.1016/S0014-5793(98)00963-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have cloned cDNAs encoding two versions of Xenopus double-stranded RNA adenosine deaminase (ADAR1). Like ADAR1 proteins from other species Xenopus ADAR1 contains three double-stranded RNA-binding domains (dsRBDs) which are most likely required for substrate binding and recognition of this RNA-editing enzyme. Analysis of mammalian ADAR1 identified the third dsRBD in this enzyme as most important for RNA binding. Here we analyzed the three dsRBDs of Xenopus ADAR1 for their in vitro RNA-binding behavior using two different assays. Northwestern assays identified the second dsRBD in the Xenopus protein as most important for RNA binding while in-solution assays demonstrated the importance of the third dsRBD for RNA binding. The differences between these two assays are discussed and we suggest that both the second and third dsRBD of Xenopus ADAR1 are important for RNA binding in vivo. We show further that all three dsRBDs can contribute to a cooperative binding effect.

【 授权许可】

Unknown