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dc.contributor.authorPons, Tirsoes_ES
dc.contributor.authorParamonov, Idaes_ES
dc.contributor.authorBoullosa, Césares_ES
dc.contributor.authorIbáñez, Kristinaes_ES
dc.contributor.authorRojas, A. M.es_ES
dc.contributor.authorValencia, Alfonsoes_ES
dc.date.accessioned2017-07-26T07:29:35Z-
dc.date.available2017-07-26T07:29:35Z-
dc.date.issued2014-01-
dc.identifier.citationProteins 82(1): 103–118 (2014)es_ES
dc.identifier.issn0887-3585-
dc.identifier.urihttp://hdl.handle.net/10261/153515-
dc.description.abstractThe phosphorylation and dephosphorylation of the carboxyl-terminal domain (CTD) of the largest RNA polymerase II (RNAPII) subunit is a critical regulatory checkpoint for transcription and mRNA processing. This CTD is unique to eukaryotic organisms and it contains multiple tandem-repeats with the consensus sequence Tyr1–Ser2–Pro3–Thr4–Ser5–Pro6–Ser7. Traditionally, CTD phosphatases that use metal-ion-independent (cysteine-based) and metal-ion-assisted (aspartate-based) catalytic mechanisms have been considered to belong to two independent groups. However, using structural comparisons we have identified a common structural scaffold in these two groups of CTD phosphatases. This common scaffold accommodates different catalytic processes with the same substrate specificity, in this case phospho-serine/threonine residues flanked by prolines. Furthermore, this scaffold provides a structural connection between two groups of protein tyrosine phosphatases (PTPs): Cys-based (classes I, II, and III) and Asp-based (class IV) PTPs. Redundancy in catalytic mechanisms is not infrequent and may arise in specific biological settings. To better understand the activity of the CTD phosphatases, we combined our structural analyses with data on CTD phosphatase expression in different human and mouse tissues. The results suggest that aspartate- and cysteine-based CTD-dephosphorylation acts in concert during cellular stress, when high levels of reactive oxygen species can inhibit the nucleophilic function of the catalytic cysteine, as occurs in mental and neurodegenerative disorders like schizophrenia, Alzheimer's and Parkinson's diseases. Moreover, these findings have significant implications for the study of the RNAPII-CTD dephosphorylation in eukaryotes. Proteins 2014; 82:103–118. © 2013 Wiley Periodicals, Inc.es_ES
dc.description.sponsorshipGrant sponsor: EU FP7 ASSET project; Grant number: 259348 (to AV); Grant sponsor: Obra Social laCaixa (to KI); Grant sponsor: FPI; Grant number: BES- 2008-006332 (to CB).es_ES
dc.language.isoenges_ES
dc.publisherWiley-Lisses_ES
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/259348es_ES
dc.rightsclosedAccesses_ES
dc.subjectStructure comparisones_ES
dc.subjectRNA poly merase II carboxyl-terminal domaines_ES
dc.subjectProtein phosphataseses_ES
dc.subjectCatalytic mechanismes_ES
dc.subjectHAD superfamilyes_ES
dc.subjectProlyl cis/trans isomerizationes_ES
dc.subjectOxidative stresses_ES
dc.subjectNeurodegenerationes_ES
dc.subjectMental disorderses_ES
dc.subjectAlzheimer’s diseasees_ES
dc.subjectParkinson’s diseasees_ES
dc.subjectSchizophreniaes_ES
dc.titleA common structural scaffold in CTD phosphatases that supports distinct catalytic mechanismses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1002/prot.24376-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://doi.org/10.1002/prot.24376es_ES
dc.identifier.e-issn1097-0134-
dc.contributor.funderEuropean Commissiones_ES
dc.contributor.funderObra Social la Caixaes_ES
dc.relation.csicNoes_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
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