Allosteric couplings upon binding of RfaH to transcription elongation complexes

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dc.contributor.authorAlejandro Molina, Jose
dc.contributor.authorGalaz-Davison, Pablo
dc.contributor.authorKomives, Elizabeth A.
dc.contributor.authorArtsimovitch, Irina
dc.contributor.authorRamirez-Sarmiento, Cesar A.
dc.date.accessioned2025-01-20T21:06:36Z
dc.date.available2025-01-20T21:06:36Z
dc.date.issued2022
dc.description.abstractIn every domain of life, NusG-like proteins bind to the elongating RNA polymerase (RNAP) to support processive RNA synthesis and to couple transcription to ongoing cellular processes. Structures of factor-bound transcription elongation complexes (TECs) reveal similar contacts to RNAP, consistent with a shared mechanism of action. However, NusG homologs differ in their regulatory roles, modes of recruitment, and effects on RNA synthesis. Some of these differences could be due to conformational changes in RNAP and NusG-like proteins, which cannot be captured in static structures. Here, we employed hydrogen-deuterium exchange mass spectrometry to investigate changes in local and non-local structural dynamics of Escherichia coli NusG and its paralog RfaH, which have opposite effects on expression of xenogenes, upon binding to TEC. We found that NusG and RfaH regions that bind RNAP became solvent-protected in factor-bound TECs, whereas RNAP regions that interact with both factors showed opposite deuterium uptake changes when bound to NusG or RfaH. Additional changes far from the factor-binding site were observed only with RfaH. Our results provide insights into differences in structural dynamics exerted by NusG and RfaH during binding to TEC, which may explain their different functional outcomes and allosteric regulation of transcriptional pausing by RfaH.
dc.fuente.origenWOS
dc.identifier.doi10.1093/nar/gkac453
dc.identifier.eissn1362-4962
dc.identifier.issn0305-1048
dc.identifier.urihttps://doi.org/10.1093/nar/gkac453
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/93358
dc.identifier.wosidWOS:000807082900001
dc.issue.numero11
dc.language.isoen
dc.pagina.final6397
dc.pagina.inicio6384
dc.revistaNucleic acids research
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAllosteric couplings upon binding of RfaH to transcription elongation complexes
dc.typeartículo
dc.volumen50
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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