HÓBOR, Fruzsina, Karel KUBÍČEK, Josef PASULKA and Richard ŠTEFL. Structure and RNA binding of Nab3. In Structure and RNA binding of Nab3. 2009. ISSN 1211-5894.
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Basic information
Original name Structure and RNA binding of Nab3
Authors HÓBOR, Fruzsina (348 Hungary), Karel KUBÍČEK (203 Czech Republic), Josef PASULKA (203 Czech Republic) and Richard ŠTEFL (203 Czech Republic, guarantor).
Edition Structure and RNA binding of Nab3, 2009.
Other information
Original language English
Type of outcome Conference abstract
Field of Study Genetics and molecular biology
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/09:00028838
Organization unit Faculty of Science
ISSN 1211-5894
Keywords in English NMR; Nab3; RNA binding ; transcription termination; structure
Changed by Changed by: prof. Mgr. Richard Štefl, Ph.D., učo 19362. Changed: 25/3/2010 18:15.
Abstract
Besides mRNA, RNA polymerase II also transcribes a subset of small nuclear and small nucleoar RNAs, and a class of intergenic and anti-sense RNAs. Termination of these transcripts requires the nuclear pre-mRNA down- regulation (Nrd)1 and the nuclear polyadenylated RNA-binding (Nab)3 proteins, and the RNA helicase Sen1. In this so-called nonpoly(A) termination pathway, the RNA-binding proteins, Nrd1 and Nab3, recognize Nrd1- and Nab3-binding sites which is an initial step in the termination and subsequent processing or degradation of these transcripts. Recent studies identified sequence motives for Nrd1 and Nab3, as the signals that direct termination and exosome-TRAMP trimming/degradation of nonpolyadenylated transcripts. It was shown that the RNA-recognition motif (RRM) of Nrd1 and Nab3 bind to the GUA[A/G] and UCUU sequences, respectively. In addition, it was demonstrated that Nrd1 and Nab3 form a stable heterodimer and bind to snoRNA terminators that contain multiple Nrd1- and Nab3- binding sequences. To fully understand the structural basis behind the RNA recognition by the Nrd1-Nab3 complex, we use multidimensional NMR spectroscopy to determine the three- dimensional structures of the individual RRMs of Nrd1 and Nab3 and the minimal Nrd1- Nab3 heterodimer alone as well as in complex with their RNA substrates.
Links
GA204/08/1212, research and development projectName: Strukturní studium interakcí mezi proteiny a RNA účastnící se v mechanismu kontroly kvality RNA
Investor: Czech Science Foundation, Structural studies of protein-RNA complexes involved in RNA quality control
IAA401630903, research and development projectName: Strukturní podstata mechanismu ukončení transkripce nepolyadenylovaných transkriptů
Investor: Academy of Sciences of the Czech Republic, Structural basis for transcription termination of nonpolyadenylated transcripts
LA08008, research and development projectName: Strukturní studium interakcí mezi bíkovinami a poškozenou RNA.
Investor: Ministry of Education, Youth and Sports of the CR, Structural studies of protein-RNA complexes involved in RNA quality control
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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