Literature DB >> 7862132

Cloning of cDNAs encoding mammalian double-stranded RNA-specific adenosine deaminase.

M A O'Connell1, S Krause, M Higuchi, J J Hsuan, N F Totty, A Jenny, W Keller.   

Abstract

Double-stranded RNA (dsRNA)-specific adenosine deaminase converts adenosine to inosine in dsRNA. The protein has been purified from calf thymus, and here we describe the cloning of cDNAs encoding both the human and rat proteins as well as a partial bovine clone. The human and rat clones are very similar at the amino acid level except at their N termini and contain three dsRNA binding motifs, a putative nuclear targeting signal, and a possible deaminase motif. Antibodies raised against the protein encoded by the partial bovine clone specifically recognize the calf thymus dsRNA adenosine deaminase. Furthermore, the antibodies can immunodeplete a calf thymus extract of dsRNA adenosine deaminase activity, and the activity can be restored by addition of pure bovine deaminase. Staining of HeLa cells confirms the nuclear localization of the dsRNA-specific adenosine deaminase. In situ hybridization in rat brain slices indicates a widespread distribution of the enzyme in the brain.

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Year:  1995        PMID: 7862132      PMCID: PMC230363          DOI: 10.1128/MCB.15.3.1389

Source DB:  PubMed          Journal:  Mol Cell Biol        ISSN: 0270-7306            Impact factor:   4.272


  51 in total

1.  Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI.

Authors:  S R Green; M B Mathews
Journal:  Genes Dev       Date:  1992-12       Impact factor: 11.361

Review 2.  Cytosine nucleoside/nucleotide deaminases and apolipoprotein B mRNA editing.

Authors:  S Bhattacharya; N Navaratnam; J R Morrison; J Scott; W R Taylor
Journal:  Trends Biochem Sci       Date:  1994-03       Impact factor: 13.807

Review 3.  The flip side of DNA methylation.

Authors:  G L Verdine
Journal:  Cell       Date:  1994-01-28       Impact factor: 41.582

4.  HhaI methyltransferase flips its target base out of the DNA helix.

Authors:  S Klimasauskas; S Kumar; R J Roberts; X Cheng
Journal:  Cell       Date:  1994-01-28       Impact factor: 41.582

5.  RNA editing of AMPA receptor subunit GluR-B: a base-paired intron-exon structure determines position and efficiency.

Authors:  M Higuchi; F N Single; M Köhler; B Sommer; R Sprengel; P H Seeburg
Journal:  Cell       Date:  1993-12-31       Impact factor: 41.582

6.  Purification and characterization of double-stranded RNA adenosine deaminase from bovine nuclear extracts.

Authors:  U Kim; T L Garner; T Sanford; D Speicher; J M Murray; K Nishikura
Journal:  J Biol Chem       Date:  1994-05-06       Impact factor: 5.157

7.  The p27 catalytic subunit of the apolipoprotein B mRNA editing enzyme is a cytidine deaminase.

Authors:  N Navaratnam; J R Morrison; S Bhattacharya; D Patel; T Funahashi; F Giannoni; B B Teng; N O Davidson; J Scott
Journal:  J Biol Chem       Date:  1993-10-05       Impact factor: 5.157

8.  Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen.

Authors:  A Gatignol; C Buckler; K T Jeang
Journal:  Mol Cell Biol       Date:  1993-04       Impact factor: 4.272

9.  Purification of the Xenopus laevis double-stranded RNA adenosine deaminase.

Authors:  R F Hough; B L Bass
Journal:  J Biol Chem       Date:  1994-04-01       Impact factor: 5.157

10.  A target for Src in mitosis.

Authors:  S Fumagalli; N F Totty; J J Hsuan; S A Courtneidge
Journal:  Nature       Date:  1994-04-28       Impact factor: 49.962

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  92 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.  Increased RNA editing and inhibition of hepatitis delta virus replication by high-level expression of ADAR1 and ADAR2.

Authors:  Geetha C Jayan; John L Casey
Journal:  J Virol       Date:  2002-04       Impact factor: 5.103

Review 4.  RNA editing by adenosine deaminases that act on RNA.

Authors:  Brenda L Bass
Journal:  Annu Rev Biochem       Date:  2001-11-09       Impact factor: 23.643

5.  Elevated activity of the large form of ADAR1 in vivo: very efficient RNA editing occurs in the cytoplasm.

Authors:  Swee Kee Wong; Shuji Sato; David W Lazinski
Journal:  RNA       Date:  2003-05       Impact factor: 4.942

6.  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

7.  A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains.

Authors:  C X Chen; D S Cho; Q Wang; F Lai; K C Carter; K Nishikura
Journal:  RNA       Date:  2000-05       Impact factor: 4.942

8.  Evidence that RNA editing modulates splice site selection in the 5-HT2C receptor gene.

Authors:  Rachel Flomen; Joanne Knight; Pak Sham; Robert Kerwin; Andrew Makoff
Journal:  Nucleic Acids Res       Date:  2004-04-15       Impact factor: 16.971

9.  Modulation of RNA editing by functional nucleolar sequestration of ADAR2.

Authors:  Christopher L Sansam; K Sam Wells; Ronald B Emeson
Journal:  Proc Natl Acad Sci U S A       Date:  2003-11-11       Impact factor: 11.205

Review 10.  Activity regulation of adenosine deaminases acting on RNA (ADARs).

Authors:  Cesare Orlandi; Alessandro Barbon; Sergio Barlati
Journal:  Mol Neurobiol       Date:  2011-11-20       Impact factor: 5.590

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