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- W4311193936 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." @default.
- W4311193936 created "2022-12-24" @default.
- W4311193936 creator A5003816215 @default.
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- W4311193936 creator A5091163197 @default.
- W4311193936 date "2022-12-01" @default.
- W4311193936 modified "2023-10-14" @default.
- W4311193936 title "Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold" @default.
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- W4311193936 doi "https://doi.org/10.3390/biom12121798" @default.
- W4311193936 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36551226" @default.
- W4311193936 hasPublicationYear "2022" @default.
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