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

Τύπος:	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	NMR Analysis suggests synergy between the RRM2 and the Carboxy-Terminal segment of Human La Protein in the recognition and Interaction with HCV IRES
Συγγραφέας:	[EL] Αργυρίου, Αικατερίνη[EN] Argyriou, Aikaterini [EL] Μαχαλιώτης, Γεώργιος[EN] Machaliotis, Georgios [EL] Μακρυνίτσα, Γαρυφαλλιά[EN] Makrynitsa, Garyfallia [EL] Καλιάτση, Ελένη[EN] Kaliatsi, Eleni [EL] Σταθόπουλος, Κωνσταντίνος[EN] Stathopoulos, Constantinos [EL] Σπυρούλιας, Γεώργιος[EN] Spyroulias, Georgios
Ημερομηνία:	16/12/2022
Περίληψη:	La protein plays a key role in processing primary transcripts, including tRNAs, by facilitating proper folding. Although La seems to recognize and bind the 3’ poly(U) tails of many artificial small RNAs, this feature is under debate for the natural ligands of La, and the exact mechanism is still unknown. Although La is mainly located in the nucleus, it can also be found in the cytoplasm, where it affects the translation of some cellular and viral mRNAs. Human La contains four distinct domains, namely La motif (LaM), two RNA recognition motifs (RRM1 and RRM2) and a variable C-terminus region. The La’s C-terminus domain recognizes the Internal Ribosome Entry Site (IRES) of viral mRNAs and promotes their translation. Until today, the role of RRM2 and the mechanism of the IRES recognition by the La protein remain elusive. Here, we present the binding study of the RRM2 domain on the HCV-IRES recognition. We performed NMR titration experiments, titrating polypeptides of the human La that contain the RRM2 domain with the IV domain of HCV-IRES. Because we wanted to study the binding properties of RRM2 domain and a possible role of the C-terminal region on La protein – HCV IRES recognition, we performed NMR titration experiments titrating polypeptides of human La protein that contain the RRM2 domain with the IV domain of HCV IRES. With a view to identifying the specific interaction sites of the RRM2-SBM (La 224-359), the RRM2-Cter (La 224-408), the RRM1-RRM2-SBM (La 105-359) and the RRM1-RRM2-Cter (La 105-408), increasing amounts of the unlabeled HCV-IRES were added to the 15N-labeled polypeptides. 1H-15N HSQC spectra were recorded after each addition to monitor the chemical shift changes of the NH resonances. The interaction among the same La’s polypeptides with the HCV-IRES were studied with ITC (Isothermal Titration Calorimetry) in parallel with NMR.
Γλώσσα:	Αγγλικά
Σελίδες:	16
DOI:	10.3390/ijms24032572
EISSN:	1422-0067
Θεματική κατηγορία:	[EL] Βιοχημεία και Μοριακή βιολογία[EN] Biochemistry and Molecular Biology
Λέξεις-κλειδιά:	La; lupus antigen; RNA-binding proteins; hepatitis C virus; IRES; RNA virus; NMR
Κάτοχος πνευματικών δικαιωμάτων:	© 2023 by the authors. Licensee MDPI, Basel, Switzerland.
Όροι και προϋποθέσεις δικαιωμάτων:	This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).
Ηλεκτρονική διεύθυνση του τεκμηρίου στον εκδότη:	https://www.mdpi.com/1422-0067/24/3/2572
Ηλεκτρονική διεύθυνση περιοδικού:	https://www.mdpi.com/journal/ijms
Τίτλος πηγής δημοσίευσης:	International Journal of Molecular Sciences
Τεύχος:	3
Τόμος:	24
Σελίδες τεκμηρίου (στην πηγή):	Article no 2572
Σημειώσεις:	The State Scholarships Foundation (MIS 5033021), the National/Greek Research Infrastructure program “INSPIRED” (MIS 5002550) and the EU HORIZON-WIDERA-2022-TALENTS01 ERA Chairs “ESPERANCE” program (Grant agreement ID: 101087215; DOI 10.3030/101087215), are acknowledged for the financial support. EU FP7 REGPOT CT-2011-285950—the “SEE-DRUG” project—is acknowledged for the purchase of UPAT’s 700 MHz NMR equipment.
Εμφανίζεται στις συλλογές:	Μεταδιδακτορικοί ερευνητές