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10.1016/j.molcel.2017.01.029 http://scihub22266oqcxt.onion/10.1016/j.molcel.2017.01.029 C5507214!5507214!28257700     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell 2017 ; 65 (5): 832-847.e4 Nephropedia Template TP {{tp|p=28257700|t=2017. Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1 |pdf=|usr=}}{{28257700}} gab.com Text Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1 JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=28257700 #FOAvip R loop, a transcription intermediate containing RNA:DNA hybrids and displaced single-stranded DNA (ssDNA), has emerged as a major source of genomic instability. RNaseH1, which cleaves the RNA in RNA:DNA hybrids, plays an important role in R loop suppression. Here, we show that replication protein A (RPA), a ssDNA-binding protein, interacts with RNaseH1 and colocalizes with both RNaseH1 and R loops in cells. In vitro, purified RPA directly enhances the association of RNaseH1 with RNA:DNA hybrids and stimulates the activity of RNaseH1 on R loops. An RPA binding-defective RNaseH1 mutant is not efficiently stimulated by RPA in vitro, fails to accumulate at R loops in cells, and loses the ability to suppress R loops and associated genomic instability. Thus, in addition to sensing DNA damage and replication stress, RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability. Twit Text FOAVip Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1 ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=28257700 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28257700 #FOAvip English Wikipedia <ref>{{Cite pmid|28257700}}</ref> Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1 #MMPMID28257700 Nguyen HD; Yadav T; Giri S; Saez B; Graubert TA; Zou L Mol Cell 2017[Mar]; 65 (5): 832-847.e4 PMID28257700show ga R loop, a transcription intermediate containing RNA:DNA hybrids and displaced single-stranded DNA (ssDNA), has emerged as a major source of genomic instability. RNaseH1, which cleaves the RNA in RNA:DNA hybrids, plays an important role in R loop suppression. Here, we show that replication protein A (RPA), a ssDNA-binding protein, interacts with RNaseH1 and colocalizes with both RNaseH1 and R loops in cells. In vitro, purified RPA directly enhances the association of RNaseH1 with RNA:DNA hybrids and stimulates the activity of RNaseH1 on R loops. An RPA binding-defective RNaseH1 mutant is not efficiently stimulated by RPA in vitro, fails to accumulate at R loops in cells, and loses the ability to suppress R loops and associated genomic instability. Thus, in addition to sensing DNA damage and replication stress, RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability. äFunctions of Replication Protein A as a Sensor of R Loops and a Regula(epmc).pdf DeepDyve Pubget Overpricing