Publication:
The Arg293 of Cryptochrome1 is responsible for the allosteric regulation of CLOCK-CRY1 binding in circadian rhythm

dc.contributor.coauthorAydın, Cihan
dc.contributor.departmentDepartment of Molecular Biology and Genetics
dc.contributor.departmentDepartment of Chemical and Biological Engineering
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.kuauthorBarış, İbrahim
dc.contributor.kuauthorGül, Şeref
dc.contributor.kuauthorKavaklı, İbrahim Halil
dc.contributor.kuauthorÖzcan, Onur
dc.contributor.kuauthorSürme, Saliha
dc.contributor.kuauthorGürkan, Berke
dc.contributor.schoolcollegeinstituteCollege of Engineering
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.date.accessioned2024-11-09T13:07:17Z
dc.date.issued2020
dc.description.abstractMammalian circadian clocks are driven by transcription/ translation feedback loops composed of positive transcriptional activators (BMAL1 and CLOCK) and negative repressors (CRYPTOCHROMEs (CRYs) and PERIODs (PERs)). CRYs, in complex with PERs, bind to the BMAL1/CLOCK complex and repress E-box-driven transcription of clock-associated genes. There are two individual CRYs, with CRY1 exhibiting higher affinity to the BMAL1/CLOCK complex than CRY2. It is known that this differential binding is regulated by a dynamic serine-rich loop adjacent to the secondary pocket of both CRYs, but the underlying features controlling loop dynamics are not known. Here we report that allosteric regulation of the serine-rich loop is mediated by Arg-293 of CRY1, identified as a rare CRY1 SNP in the Ensembl and 1000 Genomes databases. The p.Arg293His CRY1 variant caused a shortened circadian period in a Cry1-/-Cry2-/-double knockout mouse embryonic fibroblast cell line. Moreover, the variant displayed reduced repressor activity on BMAL1/CLOCK driven transcription, which is explained by reduced affinity to BMAL1/ CLOCK in the absence of PER2 compared with CRY1.Molecular dynamics simulations revealed that the p.Arg293His CRY1 variant altered a communication pathway between Arg-293 and the serine loop by reducing its dynamicity. Collectively, this study provides direct evidence that allosterism in CRY1 is critical for the regulation of circadian rhythm.
dc.description.fulltextYES
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.indexedbyWOS
dc.description.issue50
dc.description.openaccessYES
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuTÜBİTAK
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TÜBİTAK)
dc.description.sponsorshipIstanbul Development Agency Grant
dc.description.versionAuthor's final manuscript
dc.description.volume295
dc.identifier.doi10.1074/jbc.RA120.014333
dc.identifier.eissn1083-351X
dc.identifier.embargoNO
dc.identifier.filenameinventorynoIR02511
dc.identifier.issn0021-9258
dc.identifier.quartileQ2
dc.identifier.scopus2-s2.0-85097577769
dc.identifier.urihttps://doi.org/10.1074/jbc.RA120.014333
dc.identifier.wos000599868700023
dc.keywordsCircadian rhythm
dc.keywordsGene regulation
dc.keywordsCryptochrome 1
dc.keywordsAllostery
dc.keywordsCLOCK
dc.language.isoeng
dc.publisherAmerican Society for Biochemistry and Molecular Biology (ASBMB)
dc.relation.grantno114Z879
dc.relation.grantnoISTKA-TR/14/EVK/0039
dc.relation.ispartofJournal of Biological Chemistry
dc.relation.urihttp://cdm21054.contentdm.oclc.org/cdm/ref/collection/IR/id/9149
dc.subjectMolecular biology and genetics
dc.titleThe Arg293 of Cryptochrome1 is responsible for the allosteric regulation of CLOCK-CRY1 binding in circadian rhythm
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.kuauthorGül, Şeref
local.contributor.kuauthorÖzcan, Onur
local.contributor.kuauthorGürkan, Berke
local.contributor.kuauthorSürme, Saliha
local.contributor.kuauthorBarış, İbrahim
local.contributor.kuauthorKavaklı, İbrahim Halil
local.publication.orgunit1GRADUATE SCHOOL OF SCIENCES AND ENGINEERING
local.publication.orgunit1College of Engineering
local.publication.orgunit1College of Sciences
local.publication.orgunit2Department of Chemical and Biological Engineering
local.publication.orgunit2Department of Molecular Biology and Genetics
local.publication.orgunit2Graduate School of Sciences and Engineering
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