Literature DB >> 9735305

Double-stranded RNA-specific adenosine deaminase: nucleic acid binding properties.

Y Liu1, A Herbert, A Rich, C E Samuel.   

Abstract

The RNA-specific adenosine deaminase (ADAR1, herein referred to as ADAR) is an interferon-inducible RNA-editing enzyme. ADAR catalyzes the C-6 deamination of adenosine in double-stranded (ds) structures present in viral RNAs and cellular pre-mRNAs as well as synthetic dsRNA substrates. ADAR possesses three functionally distinct copies of the highly conserved double-stranded RNA binding R motif (RI, RII, RIII) implicated in the recognition of dsRNA structures within the substrate RNAs. ADAR is also a Z-DNA-binding protein. Two Z-DNA binding motifs (Zalpha and Zbeta) present in ADAR correspond to repeated regions homologous to the N-terminal region of the vaccinia virus E3L protein. Here we describe assay methods for measurement of ADAR enzymatic activity, dsRNA binding activity, and Z-DNA binding activity. Copyright 1998 Academic Press.

Entities:  

Keywords:  Non-programmatic

Mesh:

Substances:

Year:  1998        PMID: 9735305     DOI: 10.1006/meth.1998.0624

Source DB:  PubMed          Journal:  Methods        ISSN: 1046-2023            Impact factor:   3.608


  18 in total

1.  Chimeric double-stranded RNA-specific adenosine deaminase ADAR1 proteins reveal functional selectivity of double-stranded RNA-binding domains from ADAR1 and protein kinase PKR.

Authors:  Y Liu; M Lei; C E Samuel
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-07       Impact factor: 11.205

2.  The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein.

Authors:  C R Eckmann; A Neunteufl; L Pfaffstetter; M F Jantsch
Journal:  Mol Biol Cell       Date:  2001-07       Impact factor: 4.138

3.  Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain.

Authors:  Alexander Strehblow; Martina Hallegger; Michael F Jantsch
Journal:  Mol Biol Cell       Date:  2002-11       Impact factor: 4.138

Review 4.  Adenosine deaminases acting on RNA, RNA editing, and interferon action.

Authors:  Cyril X George; Zhenji Gan; Yong Liu; Charles E Samuel
Journal:  J Interferon Cytokine Res       Date:  2010-12-23       Impact factor: 2.607

Review 5.  Control of ADAR1 editing of hepatitis delta virus RNAs.

Authors:  John L Casey
Journal:  Curr Top Microbiol Immunol       Date:  2012       Impact factor: 4.291

6.  Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible.

Authors:  C X George; C E Samuel
Journal:  Proc Natl Acad Sci U S A       Date:  1999-04-13       Impact factor: 11.205

7.  The role of binding domains for dsRNA and Z-DNA in the in vivo editing of minimal substrates by ADAR1.

Authors:  A Herbert; A Rich
Journal:  Proc Natl Acad Sci U S A       Date:  2001-10-09       Impact factor: 11.205

8.  Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model.

Authors:  T A Brandt; B L Jacobs
Journal:  J Virol       Date:  2001-01       Impact factor: 5.103

Review 9.  Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral.

Authors:  Charles E Samuel
Journal:  Virology       Date:  2011-01-05       Impact factor: 3.616

10.  Effects of conserved RNA secondary structures on hepatitis delta virus genotype I RNA editing, replication, and virus production.

Authors:  Geetha C Jayan; John L Casey
Journal:  J Virol       Date:  2005-09       Impact factor: 5.103

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