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

Rishi Raj, Sharmistha Mitra, Balasubramanian Gopal

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2078-2084
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume495
Issue number2
DOIs
StatePublished - Jan 8 2018
Externally publishedYes

Keywords

  • Multi-protein assembly
  • Phosphorolysis
  • Polyadenylation
  • Ribonuclease activity
  • RNA degradation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2'. Together they form a unique fingerprint.

Cite this