TY - JOUR
T1 - RNA editing activity is associated with splicing factors in lnRNP particles
T2 - The nuclear pre-mRNA processing machinery
AU - Raitskin, Oleg
AU - Cho, Dan Sung C.
AU - Sperling, Joseph
AU - Nishikura, Kazuko
AU - Sperling, Ruth
PY - 2001/6/5
Y1 - 2001/6/5
N2 - Multiple members of the ADAR (adenosine deaminases acting on RNA) gene family are involved in A-to-I RNA editing. It has been speculated that they may form a large multicomponent protein complex. Possible candidates for such complexes are large nuclear ribonucleoprotein (lnRNP) particles. The lnRNP particles consist mainly of four spliceosomal subunits that assemble together with the pre-mRNA to form a large particle and thus are viewed as the naturally assembled pre-mRNA processing machinery. Here we investigated the presence of ADARs in lnRNP particles by Western blot analysis using anti-ADAR antibodies and by indirect immunoprecipitation. Both ADAR1 and ADAR2 were found associated with the spliceosomal components Sm and SR proteins within the lnRNP particles. The two ADARs, associated with lnRNP particles, were enzymatically active in site-selective A-to-I RNA editing. We demonstrate the association of ADAR RNA editing enzymes with physiological supramolecular complexes, the lnRNP particles.
AB - Multiple members of the ADAR (adenosine deaminases acting on RNA) gene family are involved in A-to-I RNA editing. It has been speculated that they may form a large multicomponent protein complex. Possible candidates for such complexes are large nuclear ribonucleoprotein (lnRNP) particles. The lnRNP particles consist mainly of four spliceosomal subunits that assemble together with the pre-mRNA to form a large particle and thus are viewed as the naturally assembled pre-mRNA processing machinery. Here we investigated the presence of ADARs in lnRNP particles by Western blot analysis using anti-ADAR antibodies and by indirect immunoprecipitation. Both ADAR1 and ADAR2 were found associated with the spliceosomal components Sm and SR proteins within the lnRNP particles. The two ADARs, associated with lnRNP particles, were enzymatically active in site-selective A-to-I RNA editing. We demonstrate the association of ADAR RNA editing enzymes with physiological supramolecular complexes, the lnRNP particles.
KW - Adenosine deaminases acting on RNA
KW - Double-stranded RNA adenosine deaminase
KW - Large nuclear ribonucleoprotein
KW - Nucleic acid-protein interactions
UR - http://www.scopus.com/inward/record.url?scp=0035811009&partnerID=8YFLogxK
U2 - 10.1073/pnas.111153798
DO - 10.1073/pnas.111153798
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C2 - 11381114
AN - SCOPUS:0035811009
SN - 0027-8424
VL - 98
SP - 6571
EP - 6576
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -