NMR resonance assignments of the FinO-domain of the RNA chaperone RocC

• DOI: 10.1007/s12104-020-09983-2
• Publication Date: 2020-11-11T19:02:26Z
• Authors: Reiner Eidelpes; Hyeong Jin Kim; J. N. Mark Glover; Martin Tollinger
• Keywords: 0303 health sciences; 03 medical and health sciences; Protein Domains; Bacterial Proteins; Nuclear Magnetic Resonance, Biomolecular; Article; Molecular Chaperones; Legionella pneumophila

Abstract In prokaryotic species, gene expression is commonly regulated by small, non-coding RNAs (sRNAs). the gram-negative bacterium Legionella pneumophila , regulatory, trans-acting sRNA molecule RocR base pairs with a complementary sequence in 5’-untranslated region of mRNAs encoding for proteins bacterial DNA uptake system, thereby controlling natural competence. Sense-antisense duplexing targeted mediated recently described RNA chaperone RocC. RocC contains 12 kDa FinO-domain, which acts as binding platform, along an extended C-terminal segment that predicted to be mostly disordered but appears required repression this work we assigned backbone and side chain 1 H, 13 C, 15 N chemical shifts RocC’s FinO-domain solution NMR spectroscopy. The shift data protein indicate mixed α/β fold reminiscent FinO from Escherichia coli . Our resonance assignments provide basis comprehensive analysis chaperoning mechanism on structural level.