1H, 13C, and 15N resonance assignments for the CTD-Interacting Domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA Polymerase II

• Authors: KUBÍČEK Karel; PASULKA Josef; ČERNÁ Hana; LÖHR Frank; ŠTEFL Richard
• Year of publication: 2011
• Type: Article in Periodical
• Magazine / Source: Biomolecular NMR Assignments
• MU Faculty or unit: Central European Institute of Technology
• Citation: KUBÍČEK, Karel, Josef PASULKA, Hana ČERNÁ, Frank LÖHR and Richard ŠTEFL. 1H, 13C, and 15N resonance assignments for the CTD-Interacting Domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA Polymerase II. Biomolecular NMR Assignments. Netherlands: Springer Netherlands, 2011, vol. 5, No 2, p. 203-205. ISSN 1874-2718. Available from: https://dx.doi.org/10.1007/s12104-011-9300-y.
• web: http://www.springerlink.com/content/q380231763243n87/
• Doi: http://dx.doi.org/10.1007/s12104-011-9300-y
• Field: Biophysics
• Keywords: CTD-interacting domain (CID); CTD; RNA-processing; transcription termination
• Description: In this article, we report the resonance assignment of CTD-interacting domain (CID) of pre-mRNA down-regulation (Nrd)1 bound to Ser5-phosphorylated CTD (pSer5) of RNA Polymerase II. The presented assignment of backbone and side-chain resonances of the Nrd1 CID proton, carbon and nitrogen nuclei will allow studies of the structure and interaction of CID with carboxy-terminal domain (CTD) of the RNA polymerase II

Related projects

• Proteins in metabolism and interaction of organisms with the environment
• Structural studies of protein-RNA complexes involved in RNA quality control
• Structural studies of protein-RNA complexes involved in RNA quality control
• Structural basis for transcription termination of nonpolyadenylated transcripts
• Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu