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dc.contributor.authorStrumillo, Marta J.
dc.contributor.authorOplová, Michaela
dc.contributor.authorViéitez, Cristina
dc.contributor.authorOchoa, David
dc.contributor.authorShahraz, Mohammed
dc.contributor.authorBusby, Bede P.
dc.contributor.authorSopko, Richelle
dc.contributor.authorStuder, Romain A.
dc.contributor.authorPerrimon, Norbert
dc.contributor.authorPanse, Vikram G.
dc.contributor.authorBeltrao, Pedro
dc.date.accessioned2022-03-18T16:09:39Z
dc.date.issued2019-04-29
dc.identifier.citationStrumillo, Marta J., Michaela Oplová, Cristina Viéitez, David Ochoa, Mohammed Shahraz, Bede P. Busby, Richelle Sopko et al. "Conserved phosphorylation hotspots in eukaryotic protein domain families." Nature Communications 10, no. 1 (2019): 1977. DOI: 10.1038/s41467-019-09952-x
dc.identifier.issn2041-1723en_US
dc.identifier.urihttps://nrs.harvard.edu/URN-3:HUL.INSTREPOS:37371206*
dc.description.abstractProtein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization. While the inventory for phosphorylation sites across different species has rapidly expanded, their functional role remains poorly investigated. Here, we combine 537,321 phosphosites from 40 eukaryotic species to identify highly conserved phosphorylation hotspot regions within domain families. Mapping these regions onto structural data reveals that they are often found at interfaces, near catalytic residues and tend to harbor functionally important phosphosites. Notably, functional studies of a phospho-deficient mutant in the C-terminal hotspot region within the ribosomal S11 domain in the yeast ribosomal protein uS11 shows impaired growth and defective cytoplasmic 20S pre-rRNA processing at 16 °C and 20 °C. Altogether, our study identifies phosphorylation hotspots for 162 protein domains suggestive of an ancient role for the control of diverse eukaryotic domain families.en_US
dc.language.isoen_USen_US
dc.publisherSpringer Science and Business Media LLCen_US
dc.relation.isversionofdoi:10.1038/s41467-019-09952-xen_US
dc.relation.hasversionhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6488607/en_US
dash.licensePass Through
dc.subjectGeneral Physics and Astronomyen_US
dc.subjectGeneral Biochemistry, Genetics and Molecular Biologyen_US
dc.subjectGeneral Chemistryen_US
dc.titleConserved phosphorylation hotspots in eukaryotic protein domain familiesen_US
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden_US
dc.relation.journalNature Communicationsen_US
dash.depositing.authorPerrimon, Norbert
dc.date.available2022-03-18T16:09:39Z
dc.identifier.doi10.1038/s41467-019-09952-x
dc.source.journalNat Commun
dash.source.volume10en_US
dash.source.page1977en_US
dash.source.issue1en_US
dash.contributor.affiliatedPerrimon, Norbert


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