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Vol. 12, Issue 7, 1911-1924, July 2001
Department of Cytology and Genetics, Institute of Botany,
University of Vienna, A-1030 Vienna, Austria
The RNA-editing enzyme ADAR1 (adenosine deaminase that acts on RNA)
is a bona fide nuclear enzyme that has been cloned from several
vertebrate species. Putative nuclear localization signals (NLSs) have
been identified in the aminoterminal regions of both human and
Xenopus ADAR1. Here we show that neither of these
predicted NLSs is biologically active. Instead, we could identify a
short basic region located upstream of the RNA-binding domains of
Xenopus ADAR1 to be necessary and sufficient for nuclear
import. In contrast, the homologous region in human ADAR1 does not
display NLS activity. Instead, we could map an NLS in human ADAR1 that
overlaps with its third double-stranded RNA-binding domain.
Interestingly, the NLS activity displayed by this double-stranded
RNA-binding domain does not depend on RNA binding, therefore showing a
dual function for this domain. Furthermore, nuclear accumulation of
human (hs) ADAR1 is transcription dependent and can be
stimulated by LMB, an inhibitor of Crm1-dependent nuclear export,
indicating that hsADAR1 can move between the nucleus and cytoplasm.
Regulated nuclear import and export of hsADAR1 can provide an excellent mechanism to control nuclear concentration of this editing enzyme thereby preventing hyperediting of structured nuclear RNAs.
Corresponding author. E-mail address:
Jantsch{at}s1.botanik.univie.ac.at.
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