An end-healing enzyme from Clostridium thermocellum with 5′ kinase, 2′,3′ phosphatase, and adenylyltransferase activities Journal Article
| Authors: | Martins, A.; Shuman, S. |
| Article Title: | An end-healing enzyme from Clostridium thermocellum with 5′ kinase, 2′,3′ phosphatase, and adenylyltransferase activities |
| Abstract: | We identify and characterize an end-healing enzyme, CthPnkp, from Clostridium thermocellum that catalyzes the phosphorylation of 5′-OH termini of DNA or RNA polynucleotides and the dephosphorylation of 2′,3′ cyclic phosphate, 2′-phosphate, and 3′-phosphate ribonucleotides. CthPnkp also catalyzes an autoadenylylation reaction via a polynucleotide ligase-type mechanism. These characteristics are consistent with a role in end-healing during RNA or DNA repair. CthPnkp is a homodimer of an 870-amino-acid polypeptide composed of three catalytic domains: an N-terminal module that resembles the polynucleotide kinase domain of bacteriophage T4 Pnkp, a central metal-dependent phosphoesterase module, and a C-terminal module that resembles the nucleotidyl transferase domain of polynucleotide ligases. The distinctive feature of CthPnkp vis-à-vis known RNA repair enzymes is that its 3′ end modification component belongs to the calcineurin-type phosphatase superfamily. It contains putative counterparts of the amino acids that form the dinuclear metal-binding site and the phosphate-binding site of bacteriophage λ phosphatase. As with λ phosphatase, the 2′,3′ cAMP phosphatase activity of CthPnkp is specifically dependent on nickel or manganese. We identify homologs of CthPnkp in other bacterial proteomes. Copyright © 2005 RNA Society. |
| Keywords: | protein expression; unclassified drug; nonhuman; protein domain; dna repair; phosphatase; enzyme activity; phosphorylation; bacterial proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; amino terminal sequence; kinetics; sequence alignment; nucleotide sequence; cyclic amp; binding site; catalysis; phosphotransferase; nickel; chemical reaction; protein modification; ligase; polynucleotide; adenylation; polynucleotide kinase; rna repair; dephosphorylation; nucleotidyltransferases; bacterial enzyme; clostridium thermocellum; manganese; transferase; calcineurin; bacteriophage; bacteriophage lambda; end-healing; phosphoesterase; nucleotidases; amino acid derivative; cthpnkp enzyme; phosphotransferases (phosphate group acceptor) |
| Journal Title: | RNA |
| Volume: | 11 |
| Issue: | 8 |
| ISSN: | 1355-8382 |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Date Published: | 2005-08-01 |
| Start Page: | 1271 |
| End Page: | 1280 |
| Language: | English |
| DOI: | 10.1261/rna.2690505 |
| PUBMED: | 15987807 |
| PROVIDER: | scopus |
| PMCID: | PMC1370810 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 23" - "Export Date: 24 October 2012" - "CODEN: RNARF" - "Molecular Sequence Numbers: GENBANK: AAP78353, BAB75430, EAA24876, NP_630089, YP079636, ZP_00312808, ZP_00354175;" - "Source: Scopus" |
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