Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold - Archive ouverte HAL Access content directly
Journal Articles Biomolecules Year : 2022

Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold

Abstract

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.
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Dates and versions

hal-04106119 , version 1 (25-05-2023)

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Nelly Morellet, Pierre Hardouin, Nadine Assrir, Carine van Heijenoort, Béatrice Golinelli-Pimpaneau. Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold. Biomolecules, 2022, 12 (12), pp.1798. ⟨10.3390/biom12121798⟩. ⟨hal-04106119⟩
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