Mammalian RNA-dependent deaminases and edited mRNAs.
The past year has witnessed major progress in the field of mammalian nuclear RNA editing. Two new sequence-related RNA-dependent adenosine deaminases, distantly related to the previously characterized double-stranded RNA adenosine deaminase DRADA/dsRAD, have been molecularly characterized. One of these deaminases edits in vitro with precision for the molecular determinant that controls the Ca2+ permeability of fast synaptic glutamate-gated cation channels. This deaminase, like DRADA, is expressed in many tissues and the search is now on for more substrates of these RNA-editing enzymes. Moreover, the physiological role of the apolipoprotein B RNA editing enzyme APOBEC-1 has been investigated in genetically manipulated mice.
Maas
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Department of Molecular Neurobiology, Max-Planck Institute for Medical Research, Jahnstrasse 29, 69120, Heidelberg, Germany.
Melcher
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Seeburg
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PH
D000071479:APOBEC-1 Deaminase; D000243:Adenosine Deaminase / Q000378:metabolism*; D000818:Animals; D030801:Animals, Genetically Modified; D001055:Apolipoproteins B / Q000235:genetics; D003564:Cytidine Deaminase / Q000378:metabolism*; D007473:Ion Channels / Q000235:genetics; D008322:Mammals; D051379:Mice; D017393:RNA Editing; D012333:RNA, Messenger / Q000378:metabolism; D018091:Receptors, AMPA / Q000235:genetics; D013379:Substrate Specificity; D000098830:AICDA (Activation-Induced Cytidine Deaminase)
D001055:Apolipoproteins B; D007473:Ion Channels; D012333:RNA, Messenger; D018091:Receptors, AMPA; D000098830:AICDA (Activation-Induced Cytidine Deaminase); D000071479:APOBEC-1 Deaminase; C000605090:Apobec1 protein, mouse; D000243:Adenosine Deaminase; D003564:Cytidine Deaminase; C104722:glutamate receptor ionotropic, AMPA 2