Ribonuclease III-mediated processing of specific Neisseria meningitidis mRNAs
| Autor: | Chiara Abrescia, M. Stella Carlomagno, Eliana De Gregorio, Pier Paolo Di Nocera |
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| Přispěvatelé: | DE GREGORIO, Eliana, Abrescia, Chiara, CARLOMAGNO MARIA, Stella, DI NOCERA, Pierpaolo |
| Rok vydání: | 2003 |
| Předmět: |
Ribonuclease III
DNA insertion sequence Pathogenic micro-organism Post-transcriptional control RNA hairpin Segmental RNA stability Base Sequence Endoribonucleases Molecular Sequence Data Neisseria meningitidis Nucleic Acid Conformation Open Reading Frames RNA Stability RNA Bacterial RNA Messenger Short Interspersed Nucleotide Elements Terminal Repeat Sequences RNA Processing Post-Transcriptional Biochemistry RNA Processing Inverted repeat Messenger Post-Transcriptional Cleavage (embryo) chemistry.chemical_compound Coding region Insertion sequence Molecular Biology Gene biology Bacterial RNA Cell Biology Molecular biology chemistry biology.protein DNA Research Article |
| Zdroj: | Biochemical Journal. 374:799-805 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj20030533 |
| Popis: | Approx. 2% of the Neisseria meningitidis genome consists of small DNA insertion sequences known as Correia or nemis elements, which feature TIRs (terminal inverted repeats) of 26–27 bp in length. Elements interspersed with coding regions are co-transcribed with flanking genes into mRNAs, processed at double-stranded RNA structures formed by TIRs. N. meningitidis RNase III (endoribonuclease III) is sufficient to process nemis+ RNAs. RNA hairpins formed by nemis with the same termini (26/26 and 27/27 repeats) are cleaved. By contrast, bulged hairpins formed by 26/27 repeats inhibit cleavage, both in vitro and in vivo. In electrophoretic mobility shift assays, all hairpin types formed similar retarded complexes upon incubation with RNase III. The levels of corresponding nemis+ and nemis− mRNAs, and the relative stabilities of RNA segments processed from nemis+ transcripts in vitro, may both vary significantly. |
| Databáze: | OpenAIRE |
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