Topic
Nrd1 complex
About: Nrd1 complex is a research topic. Over the lifetime, 5 publications have been published within this topic receiving 121 citations.
Papers
TL;DR: How RNA polymerase II selects which pathway to use is discussed, and stable or cryptic unstable transcripts use the Nrd1 complex, whereas mRNA uses 3′ cleavage and polyadenylation factors together with Rat1 exonuclease.
Abstract: Transcriptional termination by RNA polymerase II in yeast occurs by two different pathways: stable or cryptic unstable transcripts use the Nrd1 complex, whereas mRNA uses 3′ cleavage and polyadenylation factors together with Rat1 exonuclease. How RNA polymerase II selects which pathway to use is discussed.
20 citations
TL;DR: The structure and RNA-binding properties of Nrd1 are studied using nuclear magnetic resonance (NMR), fluorescence anisotropy and phenotypic analyses in vivo, and some transcripts do not require GUA[A/G] motif for transcription termination in vivo and binding in vitro, suggesting the existence of alternative Nrd 1-binding motifs.
Abstract: In Saccharomyces cerevisiae, the Nrd1-dependent termination and processing pathways play an important role in surveillance and processing of non-coding ribonucleic acids (RNAs). The termination and subsequent processing is dependent on the Nrd1 complex consisting of two RNA-binding proteins Nrd1 and Nab3 and Sen1 helicase. It is established that Nrd1 and Nab3 cooperatively recognize specific termination elements within nascent RNA, GUA[A/G] and UCUU[G], respectively. Interestingly, some transcripts do not require GUA[A/G] motif for transcription termination in vivo and binding in vitro, suggesting the existence of alternative Nrd1-binding motifs. Here we studied the structure and RNA-binding properties of Nrd1 using nuclear magnetic resonance (NMR), fluorescence anisotropy and phenotypic analyses in vivo. We determined the solution structure of a two-domain RNA-binding fragment of Nrd1, formed by an RNA-recognition motif and helix–loop bundle. NMR and fluorescence data show that not only GUA[A/G] but also several other G-rich and AU-rich motifs are able to bind Nrd1 with affinity in a low micromolar range. The broad substrate specificity is achieved by adaptable interaction surfaces of the RNA-recognition motif and helix–loop bundle domains that sandwich the RNA substrates. Our findings have implication for the role of Nrd1 in termination and processing of many non-coding RNAs arising from bidirectional pervasive transcription.
TL;DR: This work altered the CTD-binding specificity of Nrd1 by domain swapping and found that replacing the Nrd 1 CID with that from Rtt103 reduces binding to Rrp6/Trf4, and RNA transcripts terminated by Nrd
TL;DR: The solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element is reported, showing that the first three nucleotides of UCUU are accommodated on the β-sheet surface of Nab 3 RRM, but reveals a sequence-specific recognition only for the central cytidine and uridine.
TL;DR: This work shows that two nuclear exosome cofactors, Mpp6 and Trf4, directly and competitively interact with the Nrd1 CID and differentially regulate the association of Nrd2 with two catalytic subunits of the exosomes, and promotes the processing of NRD1-terminated transcripts preferentially by Dis3, whereas Trf 4 leads to Rrp6-dependent processing.
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2016 | 1 |
| 2014 | 1 |
| 2013 | 1 |
| 2011 | 1 |
| 2008 | 1 |