6f7t
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RNY_BACSU RNY_BACSU]] Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA (PubMed:19193632). Is also the decay-initiating endonuclease for rpsO mRNA.<ref>PMID:19193632</ref> <ref>PMID:19779461</ref> <ref>PMID:20418391</ref> <ref>PMID:22412379</ref> <ref>PMID:23504012</ref> | [[http://www.uniprot.org/uniprot/RNY_BACSU RNY_BACSU]] Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA (PubMed:19193632). Is also the decay-initiating endonuclease for rpsO mRNA.<ref>PMID:19193632</ref> <ref>PMID:19779461</ref> <ref>PMID:20418391</ref> <ref>PMID:22412379</ref> <ref>PMID:23504012</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Although RNase Y acts as the key enzyme initiating messenger RNA decay in Bacillus subtilis and likely in many other Gram-positive bacteria, its three-dimensional structure remains unknown. An antibody belonging to the rare immunoglobulin G (IgG) 2b lambdax isotype was raised against a 12-residue conserved peptide from the N-terminal noncatalytic domain of B. subtilis RNase Y (BsRNaseY) that is predicted to be intrinsically disordered. Here, we show that this domain can be produced as a stand-alone protein called Nter-BsRNaseY that undergoes conformational changes between monomeric and dimeric forms. Circular dichroism and size exclusion chromatography coupled with multiangle light scattering or with small angle x-ray scattering indicate that the Nter-BsRNaseY dimer displays an elongated form and a high content of alpha-helices, in agreement with the existence of a central coiled-coil structure appended with flexible ends, and that the monomeric state of Nter-BsRNaseY is favored upon binding the fragment antigen binding (Fab) of the antibody. The dissociation constants of the IgG/BsRNaseY, IgG/Nter-BsRNaseY, and IgG/peptide complexes indicate that the affinity of the IgG for Nter-BsRNaseY is in the nM range and suggest that the peptide is less accessible in BsRNaseY than in Nter-BsRNaseY. The crystal structure of the Fab in complex with the peptide antigen shows that the peptide adopts an elongated U-shaped conformation in which the unique hydrophobic residue of the peptide, Leu6, is completely buried. The peptide/Fab complex may mimic the interaction of a microdomain of the N-terminal domain of BsRNaseY with one of its cellular partners within the degradosome complex. Altogether, our results suggest that BsRNaseY may become accessible for protein interaction upon dissociation of its N-terminal domain into the monomeric form. | ||
| + | |||
| + | Dissociation of the Dimer of the Intrinsically Disordered Domain of RNase Y upon Antibody Binding.,Hardouin P, Velours C, Bou-Nader C, Assrir N, Laalami S, Putzer H, Durand D, Golinelli-Pimpaneau B Biophys J. 2018 Oct 26. pii: S0006-3495(18)31164-0. doi:, 10.1016/j.bpj.2018.10.016. PMID:30447990<ref>PMID:30447990</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6f7t" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:00, 2 December 2018
Crystal Structure of an Fab fragment in complex with a peptide from Bacillus subtilis RNase Y
| |||||||||||
