Chemical shift assignments of a new folded domain from yeast Pcf11

Autor: Cameron D. Mackereth, Xiaoqian Xu, Sébastien Fribourg, Natacha Pérébaskine, Lionel Minvielle-Sebastia
Přispěvatelé: East China Normal University [Shangaï] (ECNU), Acides Nucléiques : Régulations Naturelle et Artificielle (ARNA), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Université de Bordeaux (UB), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), ARN : régulations naturelle et artificielle, Université Bordeaux Segalen - Bordeaux 2-Institut Européen de Chimie et de Biologie-Institut National de la Santé et de la Recherche Médicale (INSERM)
Rok vydání: 2015
Předmět:
Saccharomyces cerevisiae Proteins
Polyadenylation
Stereochemistry
Protein subunit
[SDV]Life Sciences [q-bio]
Proton Magnetic Resonance Spectroscopy
Protein domain
Molecular Sequence Data
RNA polymerase II
Peptide
Saccharomyces cerevisiae
010402 general chemistry
Cleavage (embryo)
01 natural sciences
Biochemistry
Protein Structure
Secondary
03 medical and health sciences
Structural Biology
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
Nuclear Magnetic Resonance
Biomolecular
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
chemistry.chemical_classification
mRNA Cleavage and Polyadenylation Factors
0303 health sciences
biology
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
RNA
0104 chemical sciences
Protein Structure
Tertiary
Crystallography
chemistry
biology.protein
Precursor mRNA
Zdroj: Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.421-425. ⟨10.1007/s12104-015-9622-2⟩
ISSN: 1874-270X
DOI: 10.1007/s12104-015-9622-2⟩
Popis: The yeast protein Pcf11 is a component of the cleavage/polyadenylation factor IA (CF IA) complex involved in the 3' processing of pre-mRNA. Pcf11 interacts with RNA and the C-terminal domain (CTD) of the largest subunit of RNA polymerase II via the CTD-interaction domain (CID), and other peptide regions mediate contacts with CF IA subunits Clp1 and Rna14/Rna15. We have identified a novel domain adjacent to the CID and have determined the backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments for the bacterially produced construct. Despite the reduced sequence complexity due to numerous glutamine and leucine residues, secondary chemical shift analysis indicates that the domain is composed of three well-defined helical regions with relaxation measurements consistent with a folded independent domain. The proximity of this previously uncharacterized domain close to the N-terminal CID prompts speculation for a putative role in modulating CTD and RNA binding, or possible intermolecular contacts within CF IA.
Databáze: OpenAIRE
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