Structure-function studies of the Bacillus subtilis Ric proteins identify the Fe-S cluster-litigating residues and their roles in development and RNA processing

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dc.contributor.authorAdusei-Danso, Felix
dc.contributor.authorKhaja, Faisal Tarique
dc.contributor.authorDeSantis, Micaela
dc.contributor.authorJeffrey, Philip D.
dc.contributor.authorDubnau, Eugenie
dc.contributor.authorDemeler, Borries
dc.contributor.authorNeiditch, Matthew B.
dc.contributor.authorDubnau, David
dc.date.accessioned2021-07-05T21:27:05Z
dc.date.available2021-07-05T21:27:05Z
dc.date.issued2019
dc.descriptionOpen access article. Creative Commons Attribution 4.0 International LIcense (CC BY 4.0) appliesen_US
dc.description.abstractIn Bacillus subtilis, the RicA (YmcA), RicF (YlbF), and RicT (YaaT) proteins accelerate the phosphorylation of the transcription factor Spo0A, contributing to ge netic competence, sporulation, and biofilm formation, and are also essential for the correct maturation of several protein-encoding and riboswitch RNAs. These proteins form a stable complex (RicAFT) that carries two [4Fe-4S] 2 clusters. We show here that the complex is a 1:1:1 heterotrimer, and we present the X-ray crystal structures of a RicAF heterotetramer and of a RicA dimer. We also demonstrate that one of the Fe-S clusters (cluster 1) is ligated by cysteine residues donated exclusively by RicT and can be retained when the RicT monomer is purified by itself. Cluster 2 is ligated by C167 from RicT, by C134 and C146 located near the C terminus of RicF, and by C141 at the C terminus of RicA. These findings imply the following novel arrange ment: adjacent RicT residues C166 and 167 ligate clusters 1 and 2, respectively, while cluster 2 is ligated by cysteine residues from RicT, RicA, and RicF. Thus, the two clusters must lie close to one another and at the interface of the RicAFT protomers. We also show that the cluster-ligating cysteine residues, and therefore most likely both Fe-S clusters, are essential for cggR-gapA mRNA maturation, for the regulation of ricF transcript stability, and for several Ric-associated developmental phenotypes, including competence for transformation, biofilm formation, and sporu lation. Finally, we present evidence that RicAFT, RicAF, and RicA and the RicT mono mer may play distinct regulatory roles in vivo.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationAdusei-Danso, F., Khaja, F. T., DeSantis, M., Jeffrey, P. D., Dubnau, E., Demeler, B., Neiditch, M. B., & Dubnau, D. (2019). Structure-function studies of the Bacillus subtilis Ric proteins identify the Fe-S cluster-litigating residues and their roles in development and RNA processing. mBio, 10(5), Article e01841-19. https://doi.org/10.1128/mBio.01841-19en_US
dc.identifier.urihttps://hdl.handle.net/10133/5940
dc.language.isoen_USen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionRutgers Universityen_US
dc.publisher.institutionCenter of New Jersey Medical Schoolen_US
dc.publisher.institutionPrinceton Universityen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1128/mBio.01841-19en_US
dc.subjectRic proteinsen_US
dc.subjectIron sulfur clusteren_US
dc.subjectRNA processingen_US
dc.subjectBacterial developmenten_US
dc.subjectFe-S cluster
dc.subject.lcshBacillus subtilis
dc.titleStructure-function studies of the Bacillus subtilis Ric proteins identify the Fe-S cluster-litigating residues and their roles in development and RNA processingen_US
dc.typeArticleen_US
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