Characterization of Runella slithyformis HD-Pnk, a bifunctional DNA/RNA end-healing enzyme composed of an N-terminal 2',3'- phosphoesterase HD domain and a C-terminal 5'-OH polynucleotide kinase domain Journal Article
| Authors: | Munir, A.; Shuman, S. |
| Article Title: | Characterization of Runella slithyformis HD-Pnk, a bifunctional DNA/RNA end-healing enzyme composed of an N-terminal 2',3'- phosphoesterase HD domain and a C-terminal 5'-OH polynucleotide kinase domain |
| Abstract: | 5=- and 3=-end-healing reactions are key steps in nucleic acid break repair in which 5=-OH ends are phosphorylated by a polynucleotide kinase (Pnk) and 3=-PO4 or 2=,3=-cyclic-PO4 ends are hydrolyzed by a phosphoesterase to generate the 5=-PO4 and 3=-OH termini required for sealing by classic polynucleotide ligases. Endhealing and sealing enzymes are present in diverse bacterial taxa, often organized as modular units within a single multifunctional polypeptide or as subunits of a repair complex. Here we identify and characterize Runella slithyformis HD-Pnk as a novel bifunctional end-healing enzyme composed of an N-terminal 2=,3=-phosphoesterase HD domain and a C-terminal 5=-OH polynucleotide kinase P-loop domain. HD-Pnk phosphorylates 5=-OH polynucleotides (9-mers or longer) in the presence of magnesium and any nucleoside triphosphate donor. HD-Pnk dephosphorylates RNA 2=,3=- cyclic phosphate, RNA 3=-phosphate, RNA 2=-phosphate, and DNA 3=-phosphate ends in the presence of a transition metal cofactor, which can be nickel, copper, or cobalt. HD-Pnk homologs are present in genera from 11 bacterial phyla and are often encoded in an operon with a putative ATP-dependent polynucleotide ligase. © 2017 American Society for Microbiology. All Rights Reserved. |
| Keywords: | polynucleotide kinase; nucleic acid repair; 3= phosphatase |
| Journal Title: | Journal of Bacteriology |
| Volume: | 199 |
| Issue: | 3 |
| ISSN: | 0021-9193 |
| Publisher: | American Society for Microbiology |
| Date Published: | 2017-02-01 |
| Start Page: | e00739-16 |
| Language: | English |
| DOI: | 10.1128/jb.00739-16 |
| PROVIDER: | scopus |
| PMCID: | PMC5237116 |
| PUBMED: | 27895092 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 2 March 2017 -- Source: Scopus |
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