期刊
MOLECULAR BIOLOGY OF THE CELL
卷 17, 期 7, 页码 3211-3220出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E06-02-0162
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资金
- NCI NIH HHS [P30 CA068485, CA-68485] Funding Source: Medline
- NEI NIH HHS [EY-08126, P30 EY008126] Funding Source: Medline
- NICHD NIH HHS [P30 HD015052, HD-15052] Funding Source: Medline
- NIDDK NIH HHS [P30 DK058404, P60 DK020593, DK-58404, U24 DK059637, DK-59637, P30 DK020593] Funding Source: Medline
- NINDS NIH HHS [NS33323, R01 NS033323] Funding Source: Medline
ADAR2 is a double-stranded RNA-specific adenosine deaminase involved in the editing of mammalian RNAs by the site-specific conversion of adenosine to inosine (A-to-I). ADAR2 contains two tandem double-stranded RNA-binding motifs (dsRBMs) that are not only important for efficient editing of RNA substrates but also necessary for localizing APAR2 to nucleoli. The sequence and structural similarity of these motifs have raised questions regarding the role(s) that each dsRBM plays in ADAR2 function. Here we demonstrate that the dsRBMs of ADAR2 differ in both their ability to modulate subnuclear localization as well as to promote site-selective A-to-I conversion. Surprisingly, dsRBM1 contributes to editing activity in a substrate-dependent manner, indicating that dsRBMs recognize distinct structural determinants in each RNA substrate. Although dsRBM2 is essential for the editing of all substrates examined, a point mutation in this motif affects editing for only a subset of RNAs, suggesting that dsRBM2 uses unique sets of amino acid(s) for functional interactions with different RNA targets. The dsRBMs of ADAR2 are interchangeable for subnuclear targeting, yet such motif alterations do not support site-selective editing, indicating that the unique binding preferences of each dsRBM differentially contribute to their pleiotropic function.
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