Detailed Information on Publication Record
2011
Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein
HÓBOR, Fruzsina, Roberto PERGOLI, Karel KUBÍČEK, Dominika HROŠŠOVÁ, Veronika BAČÍKOVÁ et. al.Basic information
Original name
Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein
Authors
HÓBOR, Fruzsina (348 Hungary, belonging to the institution), Roberto PERGOLI (380 Italy, belonging to the institution), Karel KUBÍČEK (203 Czech Republic, belonging to the institution), Dominika HROŠŠOVÁ (703 Slovakia, belonging to the institution), Veronika BAČÍKOVÁ (203 Czech Republic, belonging to the institution), Michal ZIMMERMANN (203 Czech Republic, belonging to the institution), Josef PASULKA (203 Czech Republic, belonging to the institution), Ctirad HOFR (203 Czech Republic, belonging to the institution), Štěpánka VAŇÁČOVÁ (203 Czech Republic, belonging to the institution) and Richard ŠTEFL (203 Czech Republic, guarantor, belonging to the institution)
Edition
The Journal of Biological Chemistry, Am. Soc. for Biochem. and Mol. Biol. 2011, 0021-9258
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 4.773
RIV identification code
RIV/00216224:14740/11:00049398
Organization unit
Central European Institute of Technology
UT WoS
000286653200048
Keywords (in Czech)
NMR; proteinová struktura; zpracování RNA; interakce mezi proteinem a RNA; ukončení transkripce
Keywords in English
NMR; Protein structure; RNA processing; RNA-protein interaction; Transcription termination
Tags
International impact, Reviewed
Změněno: 25/3/2012 05:35, Olga Křížová
V originále
Non-coding RNA polymerase II transcripts are processed by the poly(A) independent termination pathway that requires the Nrd1 complex. The Nrd1 complex includes two RNA-binding proteins, the nuclear polyadenylated RNA-binding (Nab)3 and the nuclear pre-mRNA down-regulation (Nrd)1 that bind their specific termination elements. Here we report the solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element. The structure shows that the first three nucleotides of UCUU are accommodated on the beta-sheet surface of Nab3 RRM, but reveals a sequence specific recognition only for the central cytidine and uridine. The specific contacts we identified are important for binding affinity in vitro as well as for yeast viability. Further, we show that both RNA-binding motifs of Nab3 and Nrd1 alone bind their termination elements with a weak affinity. Interestingly, when Nab3 and Nrd1 form a heterodimer, the affinity to RNA is significantly increased due to the cooperative binding. These findings are in accordance with the model of their function in the poly(A) independent termination, in which the binding to the combined and/or repetitive termination elements elicits efficient termination.
In Czech
Článek se zabývá studiem struktury a biologické funkce RNA vázajícího proteinu Nab3 a jeho interakce s oligonukleotidem UCUU.
Links
GAP305/10/1490, research and development project |
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GA204/08/1212, research and development project |
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GD204/08/H054, research and development project |
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IAA401630903, research and development project |
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LA08008, research and development project |
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MSM0021622413, plan (intention) |
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MSM0021622415, plan (intention) |
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084316/Z/07/Z, interní kód MU |
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1642, interní kód MU |
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205872, interní kód MU |
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