1. Αποθετήριο Παραδοτέων Υποτρόφων Δράσεων ΕΣΠΑ Τριτοβάθμιας Εκπαίδευσης 2017-2023
2. Όλο το Αποθετήριο
3. Ερευνητικές ομάδες

Τύπος:	Αναρτημένη ανακοίνωση (poster)
Τίτλος:	Mapping the role of hRNase P individual protein subunits via CRISPR/Cas9
Μέλος ερευνητικής ομάδας:	[EL] Σκεπαρνιάς, Ηλίας[EN] Skeparnias, Ilias [EL] Σόκατ, Αθανάσιος-Νασίρ[EN] Shaukat, Athanasios-Nasir
Επικεφαλής ερευνητικής ομάδας:	[EL] Σταθόπουλος, Κωνσταντίνος[EN] Stathopoulos, Constantinos
Ημερομηνία:	29/05/2020
Περίληψη:	RNase P is an essential ribonucleoprotein responsible for the maturation of the 5’ leader of precursor tRNAs, 5S rRNA and specific long and small non-coding RNAs. Human nuclear RNase P consists of one catalytic RNA (H1) and 10 protein subunits (Rpps) some of which have known alternatives roles during transcription. In the present study, the viability of HeLa cells after ablation of either RPP21 or RPP29 using CRISPR/Cas9 was examined. Both proteins have been previously shown to play role on DNA damage and serve either as scaffold for recruitment of HDR proteins or non-coding RNAs to DSB sites, after depletion of their expression using siRNAs. The recent structure of the hRNase P complex revealed that RPP21 stacks between RPP29 and RPP38 and that both RPP21 and RPP29 are important for the local architecture of the wrist module of the holoenzyme. Disruption of either RPP21 or RPP29 genes resulted in undetectable expression, but did not affect cell viability. In the case of RPP21 knockout, observed morphological alterations in the edited cells were accompanied by significantly lower growth rates, indicating possible deregulation of their proliferation rates. Interestingly, and albeit their slow growth, RPP21 knockout cells survival suggests a metabolic rewiring that seems to be unaffected by the apparent RNase P deficiency. Expression of important transcription and translation factors was examined through qRT-PCR and western blot analysis and revealed significant alterations that could explain the observed phenotype. Overall, our data coincide with previous reports and support the notion that some of the protein subunits of RNase P, although important for the overall architecture of the holoenzyme, can be dispensable for cell viability, raising questions on the protein content of RNase P, under various conditions, including stress. Moreover, our observations highlight the possible alternative roles of Rpps beyond their participation in RNase P complex formation.
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:	25th Annual Meeting of the RNA Society #RNA2020
Τοποθεσία εκδήλωσης:	Virtual Conference
Ημ/νία έναρξης εκδήλωσης:	26/05/2020
Ημ/νία λήξης εκδήλωσης:	31/05/2020
Σημειώσεις:	Program : https://www2.rnasociety.org/wp-content/uploads/2020/05/RNA-2020-On-line-FINAL-DRAFT-V3.pdf Operational Programme «Human Resources Development, Education and Lifelong Learning. Co-financed by Greece and the European Union
Εμφανίζεται στις συλλογές:	Ερευνητικές ομάδες