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10.1016/j.jmb.2016.02.005 http://scihub22266oqcxt.onion/10.1016/j.jmb.2016.02.005 C4975007!4975007!26876600     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26876600&cmd=llinks): Failed to open stream: HTTP request failed! 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Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the DEAD-box RNA Helicase Dbp2 at Actively Transcribed Chromatin |pdf=|usr=}}{{26876600}} gab.com Text Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the DEAD-box RNA Helicase Dbp2 at Actively Transcribed Chromatin JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26876600 #FOAvip RNA helicases play fundamental roles in modulating RNA structures and facilitating RNA-protein (RNP) complex assembly in vivo. Previously, our laboratory demonstrated that the DEAD-box RNA helicase Dbp2 in S. cerevisiae is required to promote efficient assembly of the co-transcriptionally associated mRNA binding proteins Yra1, Nab2, and Mex67 onto poly(A) + RNA. We also found that Yra1 associates directly with Dbp2 and functions as an inhibitor of Dbp2-dependent duplex unwinding, suggestive of a cycle of unwinding and inhibition by Dbp2. To test this, we undertook a series of experiments to shed light on the order of events for Dbp2 in co-transcriptional mRNP assembly. We now show that Dbp2 is recruited to chromatin via RNA and forms a large, RNA-dependent complex with Yra1 and Mex67. Moreover, single molecule (smFRET) and bulk biochemical assays show that Yra1 inhibits unwinding in a concentration-dependent manner by preventing the association of Dbp2 with single-stranded RNA. This inhibition prevents over-accumulation of Dbp2 on mRNA and stabilization of a subset of RNA Pol II transcripts. We propose a model whereby Yra1 terminates a cycle of mRNP assembly by Dbp2. Twit Text FOAVip Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the DEAD-box RNA Helicase Dbp2 at Actively Transcribed Chromatin ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26876600 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26876600 #FOAvip English Wikipedia <ref>{{Cite pmid|26876600}}</ref> Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the DEAD-box RNA Helicase Dbp2 at Actively Transcribed Chromatin #MMPMID26876600 Ma WK; Paudel BP; Xing Z; Sabath IG; Rueda D; Tran EJ J Mol Biol 2016[Mar]; 428 (6): 1091-106 PMID26876600show ga RNA helicases play fundamental roles in modulating RNA structures and facilitating RNA-protein (RNP) complex assembly in vivo. Previously, our laboratory demonstrated that the DEAD-box RNA helicase Dbp2 in S. cerevisiae is required to promote efficient assembly of the co-transcriptionally associated mRNA binding proteins Yra1, Nab2, and Mex67 onto poly(A) + RNA. We also found that Yra1 associates directly with Dbp2 and functions as an inhibitor of Dbp2-dependent duplex unwinding, suggestive of a cycle of unwinding and inhibition by Dbp2. To test this, we undertook a series of experiments to shed light on the order of events for Dbp2 in co-transcriptional mRNP assembly. We now show that Dbp2 is recruited to chromatin via RNA and forms a large, RNA-dependent complex with Yra1 and Mex67. Moreover, single molecule (smFRET) and bulk biochemical assays show that Yra1 inhibits unwinding in a concentration-dependent manner by preventing the association of Dbp2 with single-stranded RNA. This inhibition prevents over-accumulation of Dbp2 on mRNA and stabilization of a subset of RNA Pol II transcripts. We propose a model whereby Yra1 terminates a cycle of mRNP assembly by Dbp2. äRecruitment, Duplex Unwinding and Protein-Mediated Inhibition of the D(epmc).pdf DeepDyve Pubget Overpricing