The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus

• Published in: Nucleic acids research Vol. 46; no. 3; pp. 1345 - 1361
• Main Authors: Caballero, Carlos J, Menendez-Gil, Pilar, Catalan-Moreno, Arancha, Vergara-Irigaray, Marta, García, Begoña, Segura, Víctor, Irurzun, Naiara, Villanueva, Maite, Ruiz de los Mozos, Igor, Solano, Cristina, Lasa, Iñigo, Toledo-Arana, Alejandro
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 16.02.2018
• Subjects: 5' Untranslated Regions; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Base Pairing; Binding Sites; Carbohydrate Metabolism - genetics; Feedback, Physiological; Gene Deletion; Gene Expression Regulation, Bacterial; Models, Molecular; Molecular Biology; Nucleic Acid Conformation; Protein Binding; Protein Structure, Secondary; Proteome - genetics; Proteome - metabolism; Regulon; Ribonuclease III - chemistry; Ribonuclease III - genetics; Ribonuclease III - metabolism; RNA, Bacterial; Staphylococcus aureus - genetics; Staphylococcus aureus - metabolism; Staphylococcus aureus - pathogenicity; Stress, Physiological - genetics; Virulence

Abstract RNA-binding proteins (RBPs) are essential to fine-tune gene expression. RBPs containing the cold-shock domain are RNA chaperones that have been extensively studied. However, the RNA targets and specific functions for many of them remain elusive. Here, combining comparative proteomics and RB...