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https://hdl.handle.net/123456789/1641| Τύπος: | Αναρτημένη ανακοίνωση (poster) |
| Τίτλος: | CRISPR/Cas9 screening of hRNase P protein subunits |
| Συγγραφέας: | [EL] Καλιάτση, Ελένη[EN] Kaliatsi, Eleni |
| Μέλος ερευνητικής ομάδας: | [EL] Σόκατ, Αθανάσιος-Νασίρ[EN] Shaukat, Athanasios-Nasir [EL] Σκεπαρνιάς, Ηλίας[EN] Skeparnias, Ilias |
| Επικεφαλής ερευνητικής ομάδας: | [EL] Σταθόπουλος, Κωνσταντίνος[EN] Stathopoulos, Constantinos |
| Ημερομηνία: | 01/06/2021 |
| Περίληψη: | Human RNase P, the essential ribonuclease for processing the 5’ leader of precursor tRNAs consists of a sole RNA and ten protein subunits, some of which have been reported with moonlighting functions. The recent structure of the holoenzyme informs for detailed involvement of specific protein subunits in tRNA binding and catalysis, while the role of protein-protein interactions between specific subunits in the binding of other RNAs and their role in RNPs like RNase MRP, was also suggested. To clarify the essentiality or redundancy of each protein subunit we screened HeLa cells using CRISPR/Cas9 genome editing for the role of RPP21 (3 alleles), RPP25 (2 alleles), RPP29 (2 alleles) and POP1 (3 alleles) subunits. Ablation of POP1 leads to lethality, thus confirming its central role as a core component of several important RNPs, beyond RNase P, RNase MRP, and telomerase (in yeast). On the other hand, successful editing of RPP21 , RPP25 or RPP29, leading to undetectable protein levels, suggests that these subunits are dispensable for cell viability. More specifically, HeLa cells with confirmed RPP21 and RPP29 knockout, exhibited morphological alterations, accompanied by lower growth rate, a finding that was not observed after RPP25 ablation. Cell cycle analysis of edited cells showed that RPP21 or RPP29 deletion results in a higher G2-M phase arrest, whereas RPP25 deletion leads to a G1 phase arrest. In addition, knockout of each subunit leads to aberrant signaling and lower translation rates in HeLa cells. Given that RPP21 and RPP29 are recruited to double-stranded breaks, the observed cell cycle arrest of edited cells agrees with their alternative roles and suggests a possible correlation between protein synthesis rate and cell proliferation. Current and previous reports are supportive of the notion that specific individual protein subunits of RNase P, although important for the overall architecture of the holoenzyme, can be dispensable for cell viability, raising questions on the minimum protein content of RNase P (and possibly other RNPs) under conditions like stress. Moreover, our observations highlight the possible alternative roles of RPPs beyond their participation in RNP complexes. |
| Γλώσσα: | Αγγλικά |
| Τόπος δημοσίευσης: | Virtually |
| Σελίδες: | 1 |
| Θεματική κατηγορία: | [EL] Βιοχημεία και Μοριακή βιολογία[EN] Biochemistry and Molecular Biology |
| Λέξεις-κλειδιά: | Ribonuclease P; RNase P |
| Κάτοχος πνευματικών δικαιωμάτων: | © RNA Society |
| Όνομα εκδήλωσης: | 26th Annual Meeting of the RNA Society (#RNA 2021) |
| Τοποθεσία εκδήλωσης: | Virtual Conference |
| Ημ/νία έναρξης εκδήλωσης: | 25/05/2021 |
| Ημ/νία λήξης εκδήλωσης: | 04/06/2021 |
| Σημειώσεις: | Program : https://www2.rnasociety.org/wp-content/uploads/2021/05/RNA-2021-Program-1.pdf Operational Programme «Human Resources Development, Education and Lifelong Learning. Co-financed by Greece and the European Union |
| Εμφανίζεται στις συλλογές: | Ερευνητικές ομάδες |
Αρχεία σε αυτό το τεκμήριο:
| Αρχείο | Περιγραφή | Σελίδες | Μέγεθος | Μορφότυπος | Έκδοση | Άδεια | |
|---|---|---|---|---|---|---|---|
| POSTER RNA 2021.pdf | 4.56 MB | Adobe PDF | - |  | Δείτε/ανοίξτε |