Structural highlights
Function
[PNP_STAES] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Publication Abstract from PubMed
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.
Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2.,Raj R, Mitra S, Gopal B Biochem Biophys Res Commun. 2018 Jan 8;495(2):2078-2084. doi:, 10.1016/j.bbrc.2017.12.056. Epub 2017 Dec 11. PMID:29242153[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Raj R, Mitra S, Gopal B. Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2. Biochem Biophys Res Commun. 2018 Jan 8;495(2):2078-2084. doi:, 10.1016/j.bbrc.2017.12.056. Epub 2017 Dec 11. PMID:29242153 doi:http://dx.doi.org/10.1016/j.bbrc.2017.12.056
