Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2

Raj, Rishi and Mitra, Sharmistha and Gopal, Balasubramanian (2018) Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2. In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 495 (2). pp. 2078-2084.

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Abstract

Polynucleotide phosphorylase catalyzes both 3'-5' exoribonuclease and polyadenylation reactions. The crystal structure of Staphylococcus epidermidis PNPase revealed a bound phosphate in the PH2 domain of each protomer coordinated by three adjacent serine residues. Mutational analysis suggests that phosphate coordination by these serine residues is essential to maintain the catalytic center in an active conformation. We note that PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of this enzyme. This decoupling of catalytic activity from protein-protein interactions suggests that association of these endo-or exo-ribonucleases with PNPase could be more relevant for cellular localization or concerted targeting of structured RNA for recycling. (C) 2017 Elsevier Inc. All rights reserved.

Item Type:	Journal Article
Publication:	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Publisher:	ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
Additional Information:	Copy right for the article belong to ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	08 Mar 2018 19:06
Last Modified:	08 Mar 2018 19:06
URI:	http://eprints.iisc.ac.in/id/eprint/59136

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