| Grant number: | 17/03052-2 |
| Support type: | Scholarships in Brazil - Doctorate |
| Effective date (Start): | June 01, 2017 |
| Effective date (End): | March 07, 2021 |
| Field of knowledge: | Biological Sciences - Biochemistry - Molecular Biology |
| Cooperation agreement: | Coordination of Improvement of Higher Education Personnel (CAPES) |
| Principal researcher: | Tie Koide |
| Grantee: | Alan Péricles Rodrigues Lorenzetti |
| Home Institution: | Faculdade de Medicina de Ribeirão Preto (FMRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil |
| Associated scholarship(s): | 19/13440-5 - Detection of Insertion Sequence-encoded transposases using proteome data, BE.EP.DR |
Abstract Insertion sequences (IS) are ubiquitous mobile genetic elements in prokaryotes that promote great impact on host genomes. They can provide fitness to organisms by enhancing the genetic diversity and also by modulating gene expression. On the other hand, mobilization events that damage the host are also common, specially when an essential gene is disrupted and compromises the organism viability. Several regulatory mechanisms act to keep low transposition levels, avoiding the deleterious effects of random insertions. In bacteria, antisense RNAs and Hfq protein bind to transposase-encoding messenger RNAs (mRNAs) of IS200/IS605 family elements, preventing the translation and therefore, maintaining low levels of transposase in the cell. In archaea, LSm protein - Hfq's homologue - apparently plays a similar role, although little is known in the third domain of life. Our research team have been studying non-coding RNAs (ncRNAs) in Halobacterium salinarum NRC-1, some of them in the IS context. We analyzed LSm-RNA coimunoprecitation sequencing data from a pilot experiment in H. salinarum, and preliminary results point out that about 85% of intact IS produce transcripts that interact with this protein. In this doctoral research project, we propose the following goals: (i) identify IS-derived sense and antisense RNAs; (ii) characterize their interaction with LSm protein; (iii) identify putative targets of regulation; and (iv) elucidate their secondary structure computationally and experimentally. All these tasks will be performed for H. salinarum NRC-1, our model organism. The prevalence, conservation and specificity of LSm/Hfq-ncRNA interaction across prokaryotes will be analyzed, adding to the comprehension of transposon regulation at the post-transcriptional level. (AU) | |
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