PMID- 10430867
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 16
DP  - 1999 Aug 3
TI  - Identification and characterization of a human tRNA-specific adenosine deaminase 
      related to the ADAR family of pre-mRNA editing enzymes.
PG  - 8895-900
AB  - The mammalian adenosine deaminases acting on RNA (ADARs) constitute a family of
      sequence-related proteins involved in pre-mRNA editing of nuclear transcripts
      through site-specific adenosine modification. We report here the identification
      and characterization of a human ADAR protein, hADAT1, that specifically
      deaminates adenosine 37 to inosine in eukaryotic tRNA(Ala). It represents the
      functional homologue of the recently identified yeast protein Tad1p [Gerber, A., 
      Grosjean, H., Melcher, T. & Keller, W. (1998) EMBO J. 17, 4780-4789]. The hADAT1 
      cDNA predicts a protein of 502 aa whose sequence displays strongest overall
      homology to a Drosophila melanogaster ORF (50% similarity, 32% identity), and the
      catalytic domain is closely related to the other ADAR proteins. In vitro, the
      recombinantly expressed and purified hADAT1 protein efficiently and specifically 
      deaminates A(37) in the anticodon loop of tRNA(Ala) from higher eukaryotes and
      with lower efficiency from lower eukaryotes. It does not modify adenosines
      residing in double-stranded RNA or in pre-mRNAs that serve as substrates for
      ADAR1 or ADAR2. The anticodon stem-loop of tRNA(Ala) alone is not a functional
      substrate for hADAT1. The enzyme is expressed ubiquitously in human tissues and
      is represented by a single gene. The identification and cloning of hADAT1 should 
      help to elucidate the physiological significance of this unique modification in
      tRNA(Ala), which is conserved from yeast to man.
FAU - Maas, S
AU  - Maas S
AD  - Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts
      Avenue, MA 02139, USA.
FAU - Gerber, A P
AU  - Gerber AP
FAU - Rich, A
AU  - Rich A
LA  - eng
SI  - GENBANK/AF125188
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Anticodon)
RN  - 0 (RNA Precursors)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Transfer, Ala)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.5.4.4 (ADARB1 protein, human)
RN  - EC 3.5.4.4 (Adenosine Deaminase)
SB  - IM
SB  - S
MH  - Adenosine Deaminase/chemistry/*genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Anticodon/metabolism
MH  - Cloning, Molecular
MH  - Drosophila melanogaster/genetics
MH  - Humans
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Organ Specificity
MH  - *RNA Editing
MH  - RNA Precursors/genetics/metabolism
MH  - RNA, Messenger/genetics
MH  - RNA, Transfer, Ala/genetics/*metabolism
MH  - RNA-Binding Proteins
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Transcription, Genetic
PMC - PMC17704
OTO - NASA
OT  - Non-programmatic
EDAT- 1999/08/04 00:00
MHDA- 1999/08/04 00:01
CRDT- 1999/08/04 00:00
PHST- 1999/08/04 00:00 [pubmed]
PHST- 1999/08/04 00:01 [medline]
PHST- 1999/08/04 00:00 [entrez]
AID - 10.1073/pnas.96.16.8895 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8895-900. doi:
      10.1073/pnas.96.16.8895.