Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs Export

@article{citeulike:1613388, abstract = {Pop6 and Pop7 are protein subunits of Saccharomyces cerevisiae RNase MRP and RNase P. Here we show that bacterially expressed Pop6 and Pop7 form a soluble heterodimer that binds the RNA components of both RNase MRP and RNase P. Footprint analysis of the interaction between the Pop6/7 heterodimer and the RNase MRP RNA, combined with gel mobility assays, demonstrates that the Pop6/7 complex binds to a conserved region of the P3 domain. Binding of these proteins to the MRP RNA leads to local rearrangement in the structure of the P3 loop and suggests that direct interaction of the Pop6/7 complex with the P3 domain of the RNA components of RNases MRP and P may mediate binding of other protein components. These results suggest a role for a key element in the RNase MRP and RNase P RNAs in protein binding, and demonstrate the feasibility of directly studying RNAprotein interactions in the eukaryotic RNases MRP and P complexes. 10.1261/rna.654407}, author = {Perederina, Anna and Esakova, Olga and Koc, Hasan and Schmitt, Mark E. and Krasilnikov, Andrey S.}, citeulike-article-id = {1613388}, citeulike-linkout-0 = {http://dx.doi.org/10.1261/rna.654407}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17717080}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17717080}, day = {23}, doi = {10.1261/rna.654407}, journal = {RNA}, keywords = {binding, domain, rna, rnasep, site, yeast}, month = {August}, pages = {rna.654407+}, posted-at = {2007-09-02 07:31:22}, priority = {5}, title = {Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs}, url = {http://dx.doi.org/10.1261/rna.654407}, year = {2007} }

TY - JOUR ID - citeulike:1613388 L3 - citeulike-article-id:1613388 N2 - Pop6 and Pop7 are protein subunits of Saccharomyces cerevisiae RNase MRP and RNase P. Here we show that bacterially expressed Pop6 and Pop7 form a soluble heterodimer that binds the RNA components of both RNase MRP and RNase P. Footprint analysis of the interaction between the Pop6/7 heterodimer and the RNase MRP RNA, combined with gel mobility assays, demonstrates that the Pop6/7 complex binds to a conserved region of the P3 domain. Binding of these proteins to the MRP RNA leads to local rearrangement in the structure of the P3 loop and suggests that direct interaction of the Pop6/7 complex with the P3 domain of the RNA components of RNases MRP and P may mediate binding of other protein components. These results suggest a role for a key element in the RNase MRP and RNase P RNAs in protein binding, and demonstrate the feasibility of directly studying RNAprotein interactions in the eukaryotic RNases MRP and P complexes. 10.1261/rna.654407 JF - RNA TI - Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs SP - rna.654407 KW - binding KW - domain KW - rna KW - rnasep KW - site KW - yeast AU - Perederina, Anna AU - Esakova, Olga AU - Koc, Hasan AU - Schmitt, Mark AU - Krasilnikov, Andrey PY - 2007/08/23/ UR - http://dx.doi.org/10.1261/rna.654407 ER -