Structural Insights into the Dimeric Form ...
Type de document :
Compte-rendu et recension critique d'ouvrage
DOI :
Titre :
Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold
Auteur(s) :
Morellet, Nelly [Auteur]
Institut de Chimie des Substances Naturelles [ICSN]
Hardouin, Pierre [Auteur]
Marrow Adiposity & Bone Lab - Adiposité Médullaire et Os - ULR 4490 [MABLab (ex-pmoi)]
Université du Littoral Côte d'Opale [ULCO]
Assrir, Nadine [Auteur]
Institut de Chimie des Substances Naturelles [ICSN]
van Heijenoort, Carine [Auteur]
Institut de Chimie des Substances Naturelles [ICSN]
Golinelli-Pimpaneau, Béatrice [Auteur]
Laboratoire de Chimie des Processus Biologiques [LCPB]
Institut de Chimie des Substances Naturelles [ICSN]
Hardouin, Pierre [Auteur]
Marrow Adiposity & Bone Lab - Adiposité Médullaire et Os - ULR 4490 [MABLab (ex-pmoi)]
Université du Littoral Côte d'Opale [ULCO]
Assrir, Nadine [Auteur]
Institut de Chimie des Substances Naturelles [ICSN]
van Heijenoort, Carine [Auteur]
Institut de Chimie des Substances Naturelles [ICSN]
Golinelli-Pimpaneau, Béatrice [Auteur]
Laboratoire de Chimie des Processus Biologiques [LCPB]
Titre de la revue :
Biomolecules
Pagination :
1798
Éditeur :
MDPI
Date de publication :
2022-12-01
ISSN :
2218-273X
Mot(s)-clé(s) en anglais :
AlphaFold
coiled-coil
structure
dimerization
RNase Y
ribonuclease
NMR
coiled-coil
structure
dimerization
RNase Y
ribonuclease
NMR
Discipline(s) HAL :
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Bactériologie
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Bactériologie
Résumé en anglais : [en]
RNase Y is a crucial component of genetic translation, acting as the key enzyme initiating mRNA decay in many Gram-positive bacteria. The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact ...
Lire la suite >RNase Y is a crucial component of genetic translation, acting as the key enzyme initiating mRNA decay in many Gram-positive bacteria. The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact with various protein partners within a degradosome complex. Bioinformatics and biophysical analysis have previously shown that Nter-BsRNaseY, which is in equilibrium between a monomeric and a dimeric form, displays an elongated fold with a high content of α-helices. Using multidimensional heteronuclear NMR and AlphaFold models, here, we show that the Nter-BsRNaseY dimer is constituted of a long N-terminal parallel coiled-coil structure, linked by a turn to a C-terminal region composed of helices that display either a straight or bent conformation. The structural organization of the N-terminal domain is maintained within the AlphaFold model of the full-length RNase Y, with the turn allowing flexibility between the N- and C-terminal domains. The catalytic domain is globular, with two helices linking the KH and HD modules, followed by the C-terminal region. This latter region, with no function assigned up to now, is most likely involved in the dimerization of B. subtilis RNase Y together with the N-terminal coiled-coil structure.Lire moins >
Lire la suite >RNase Y is a crucial component of genetic translation, acting as the key enzyme initiating mRNA decay in many Gram-positive bacteria. The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact with various protein partners within a degradosome complex. Bioinformatics and biophysical analysis have previously shown that Nter-BsRNaseY, which is in equilibrium between a monomeric and a dimeric form, displays an elongated fold with a high content of α-helices. Using multidimensional heteronuclear NMR and AlphaFold models, here, we show that the Nter-BsRNaseY dimer is constituted of a long N-terminal parallel coiled-coil structure, linked by a turn to a C-terminal region composed of helices that display either a straight or bent conformation. The structural organization of the N-terminal domain is maintained within the AlphaFold model of the full-length RNase Y, with the turn allowing flexibility between the N- and C-terminal domains. The catalytic domain is globular, with two helices linking the KH and HD modules, followed by the C-terminal region. This latter region, with no function assigned up to now, is most likely involved in the dimerization of B. subtilis RNase Y together with the N-terminal coiled-coil structure.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
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