The catalytic domain of RNase E shows inherent 3′ to 5′ directionality in cleavage site selection
RNase E, a multifunctional endoribonuclease of Escherichia coli, attacks substrates at highly specific sites. By using synthetic oligoribonucleotides containing repeats of identical target sequences protected from cleavage by 2′-O-methylated nucleotide substitutions at specific positions, we investi...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2002
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC137490/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12417756/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.202590899 |
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