MAW point mutation impairs H. Seropedicae RecA ATP hydrolysis and DNA repair without inducing large conformational changes in its structure

• Published in: PloS one Vol. 14; no. 4; p. e0214601
• Main Authors: Leite, Wellington C, Penteado, Renato F, Gomes, Fernando, Iulek, Jorge, Etto, Rafael M, Saab, Sérgio C, Steffens, Maria B R, Galvão, Carolina W
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 18.04.2019; Public Library of Science (PLoS)
• Subjects: Adenosine diphosphate; Adenosine triphosphatase; Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Amino Acid Motifs; ATP; ATPases; Bacteria; Bacterial genetics; Binding Sites; Biochemistry; Bonds (Securities); Chemistry; Core loss; Deoxyribonucleic acid; DNA; DNA binding; DNA Repair; DNA, Single-Stranded - metabolism; E coli; Escherichia coli; Escherichia coli - metabolism; Escherichia coli - radiation effects; Gene mutation; Genetic aspects; Genetic research; Herbaspirillum - genetics; Hydrogen; Hydrogen bonds; Hydrolysis; Hydrophobicity; In vivo methods and tests; MMS (Multimedia messaging service); Molecular biology; Molecular dynamics; Molecular Dynamics Simulation; Mutation; Phenotypes; Physiological aspects; Point Mutation; Protein Binding; Protein Structure, Tertiary; Proteins; Proteobacteria; Rec A Recombinases - chemistry; Rec A Recombinases - genetics; Rec A Recombinases - metabolism; RecA protein; RecA proteins; Repair; Ultraviolet Rays; Brazil; United States > US; California

RecA is a multifunctional protein that plays a central role in DNA repair in bacteria. The structural Make ATP Work motif (MAW) is proposed to control the ATPase activity of RecA. In the present work, we report the biochemical activity and structural effects of the L53Q mutation at the MAW motif of...