Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-19977
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dc.contributor.authorDelucchi, Matteo-
dc.contributor.authorSchaper, Elke-
dc.contributor.authorSachenkova, Oxana-
dc.contributor.authorElofsson, Arne-
dc.contributor.authorAnisimova, Maria-
dc.date.accessioned2020-04-30T09:00:39Z-
dc.date.available2020-04-30T09:00:39Z-
dc.date.issued2020-04-09-
dc.identifier.issn2073-4425de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/19977-
dc.description.abstractProtein tandem repeats (TRs) are often associated with immunity-related functions and diseases. Since that last census of protein TRs in 1999, the number of curated proteins increased more than seven-fold and new TR prediction methods were published. TRs appear to be enriched with intrinsic disorder and vice versa. The significance and the biological reasons for this association are unknown. Here, we characterize protein TRs across all kingdoms of life and their overlap with intrinsic disorder in unprecedented detail. Using state-of-the-art prediction methods, we estimate that 50.9% of proteins contain at least one TR, often located at the sequence flanks. Positive linear correlation between the proportion of TRs and the protein length was observed universally, with Eukaryotes in general having more TRs, but when the difference in length is taken into account the difference is quite small. TRs were enriched with disorder-promoting amino acids and were inside intrinsically disordered regions. Many such TRs were homorepeats. Our results support that TRs mostly originate by duplication and are involved in essential functions such as transcription processes, structural organization, electron transport and iron-binding. In viruses, TRs are found in proteins essential for virulence.de_CH
dc.language.isoende_CH
dc.publisherMDPIde_CH
dc.relation.ispartofGenesde_CH
dc.rightshttp://creativecommons.org/licenses/by/4.0/de_CH
dc.subjectSwiss-Protde_CH
dc.subjectDomain repeatde_CH
dc.subjectHomorepeatde_CH
dc.subjectIntrinsic disorderde_CH
dc.subjectProtein functionde_CH
dc.subjectProtein repeatde_CH
dc.subjectRepeat predictionde_CH
dc.subjectTandem repeatde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleA new census of protein tandem repeats and their relationship with intrinsic disorderde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Angewandte Simulation (IAS)de_CH
dc.identifier.doi10.3390/genes11040407de_CH
dc.identifier.doi10.21256/zhaw-19977-
dc.identifier.pmid32283633de_CH
zhaw.funding.euinfo:eu-repo/grantAgreement/EC/H2020/823886//Repeat protein Function Refinement, Annotation and Classification of Topologies/REFRACTde_CH
zhaw.issue4de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.start407de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume11de_CH
zhaw.publication.reviewOpen peer reviewde_CH
zhaw.funding.snf174836de_CH
zhaw.webfeedComputational Genomicsde_CH
zhaw.funding.zhawEU MSCA REFRACT: Repeat protein Function, Refinement, Annotation and Classification of Topologiesde_CH
zhaw.author.additionalNode_CH
zhaw.display.portraitYesde_CH
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