| Autor: |
Audrey Dorléans, Léna Zig, Inès Li de la Sierra-Gallay, Ciarán Condon, Laetitia Gilet, Harald Putzer, Jérémie Piton |
| Rok vydání: |
2011 |
| Předmět: |
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| Zdroj: |
Structure. 19(9):1252-1261 |
| ISSN: |
0969-2126 |
| DOI: |
10.1016/j.str.2011.06.018 |
| Popis: |
RNase J is a key member of the β-CASP family of metallo-β-lactamases involved in the maturation and turnover of RNAs in prokaryotes. The B. subtilis enzyme possesses both 5'-3' exoribonucleolytic and endonucleolytic activity, an unusual property for a ribonuclease. Here, we present the crystal structure of T. thermophilus RNase J bound to a 4 nucleotide RNA. The structure reveals an RNA-binding channel that illustrates how the enzyme functions in 5'-3' exoribonucleolytic mode and how it can function as an endonuclease. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode. We show that B. subtilis RNase J1, which shows processive behavior on long RNAs, behaves distributively for substrates less than 5 nucleotides in length. We propose a model involving the binding of the RNA to the surface of the β-CASP domain to explain the enzyme's processive action. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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