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Structural and biochemical characteristics of two Staphylococcus epidermidis RNase J paralogs RNase J1 and RNase J2

Raj, R and Nadig, S and Patel, T and Gopal, B (2020) Structural and biochemical characteristics of two Staphylococcus epidermidis RNase J paralogs RNase J1 and RNase J2. In: Journal of Biological Chemistry, 295 (49). pp. 16863-16876.

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Official URL: https://10.1074/jbc.RA120.014876


RNase J enzymes are metallohydrolases that are involved in RNA maturation and RNA recycling, govern gene expression in bacteria, and catalyze both exonuclease and endonuclease activity. The catalytic activity of RNase J is regulated by multiple mechanisms which include oligomerization, conformational changes to aid substrate recognition, and the metal cofactor at the active site. However, little is known of how RNase J paralogs differ in expression and activity. Here we describe structural and biochemical features of two Staphylococcus epidermidis RNase J paralogs, RNase J1 and RNase J2. RNase J1 is a homodimer with exonuclease activity aided by two metal cofactors at the active site. RNase J2, on the other hand, has endonuclease activity and one metal ion at the active site and is predominantly a monomer.Wenote that the expression levels of these enzymes vary across Staphylococcal strains. Together, these observations suggest that multiple interacting RNase J paralogs could provide a strategy for functional improvisation utilizing differences in intracellular concentration, quaternary structure, and distinct active site architecture despite overall structural similarity. © 2020 American Society for Biochemistry and Molecular Biology Inc.. All rights reserved.

Item Type: Journal Article
Publication: Journal of Biological Chemistry
Publisher: American Society for Biochemistry and Molecular Biology Inc.
Additional Information: The copyright for this article belongs to the Author(s).
Keywords: Enzymes; Gene expression; Metal ions; Metals; RNA, Biochemical characteristics; Distinct active sites; Endonuclease activities; Intracellular concentration; Staphylococcal strains; Staphylococcus epidermidis; Structural similarity; Substrate recognition, Catalyst activity, bacterial enzyme; endonuclease; exonuclease; ribonuclease J1; ribonuclease J2; unclassified drug; bacterial protein; recombinant protein; ribonuclease; RNA, Article; bacterial strain; binding site; controlled study; enzyme activity; enzyme structure; nonhuman; priority journal; protein expression; protein function; protein interaction; Staphylococcus epidermidis; biocatalysis; biosynthesis; chemistry; classification; coenzyme; dimerization; enzyme active site; enzyme specificity; enzymology; gene expression regulation; genetics; isolation and purification; metabolism; molecular dynamics; phylogeny; protein quaternary structure; site directed mutagenesis; X ray crystallography, Bacterial Proteins; Biocatalysis; Catalytic Domain; Coenzymes; Crystallography, X-Ray; Dimerization; Gene Expression Regulation, Bacterial; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Phylogeny; Protein Structure, Quaternary; Recombinant Proteins; Ribonucleases; RNA; Staphylococcus epidermidis; Substrate Specificity
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 09 Jan 2023 09:50
Last Modified: 09 Jan 2023 09:50
URI: https://eprints.iisc.ac.in/id/eprint/78954

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