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dc.contributor.authorBradley, Sean P.
dc.contributor.authorKaminski, Denise A.
dc.contributor.authorPeters, Antoine H. F. M.
dc.contributor.authorJenuwein, Thomas
dc.contributor.authorStavnezer, Janet
dc.date2022-08-11T08:11:04.000
dc.date.accessioned2022-08-23T17:31:03Z
dc.date.available2022-08-23T17:31:03Z
dc.date.issued2006-07-15
dc.date.submitted2007-09-14
dc.identifier.citation<p>J Immunol. 2006 Jul 15;177(2):1179-88.</p>
dc.identifier.issn0022-1767 (Print)
dc.identifier.doi10.4049/jimmunol.177.2.1179
dc.identifier.pmid16818776
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50645
dc.description.abstractAb class (isotype) switching allows the humoral immune system to adaptively respond to different infectious organisms. Isotype switching occurs by intrachromosomal DNA recombination between switch (S) region sequences associated with C(H) region genes. Although isotype-specific transcription of unrearranged (germline) C(H) genes is required for switching, recent results suggest that isotype specificity is also determined by the sequences of downstream (acceptor) S regions. In the current study, we identify the histone methyltransferase Suv39h1 as a novel Salpha-specific factor that specifically increases IgA switching (Smu-Salpha recombination) in a transiently transfected plasmid S substrate, and demonstrate that this effect requires the histone methyltransferase activity of Suv39h1. Additionally, B cells from Suv39h1-deficient mice have an isotype-specific reduction in IgA switching with no effect on the level of germline Ialpha-Calpha transcripts. Taken together, our results suggest that Suv39h1 activity inhibits the activity of a sequence-specific DNA-binding protein that represses switch recombination to IgA.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16818776&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.4049/jimmunol.177.2.1179
dc.subjectAnimals
dc.subjectB-Cell-Specific Activator Protein
dc.subjectB-Lymphocytes
dc.subjectBinding Sites
dc.subjectCells, Cultured
dc.subjectHistone-Lysine
dc.subjectN-Methyltransferase
dc.subjectImmunoglobulin A
dc.subject*Immunoglobulin Class Switching
dc.subjectMethyltransferases
dc.subjectMice
dc.subjectMice, Inbred C57BL
dc.subjectMice, Knockout
dc.subjectPlasmids
dc.subject*Recombination, Genetic
dc.subjectRepressor Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.subjectWomen's Studies
dc.titleThe histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA
dc.typeJournal Article
dc.source.journaltitleJournal of immunology (Baltimore, Md. : 1950)
dc.source.volume177
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/wfc_pp/171
dc.identifier.contextkey367632
html.description.abstract<p>Ab class (isotype) switching allows the humoral immune system to adaptively respond to different infectious organisms. Isotype switching occurs by intrachromosomal DNA recombination between switch (S) region sequences associated with C(H) region genes. Although isotype-specific transcription of unrearranged (germline) C(H) genes is required for switching, recent results suggest that isotype specificity is also determined by the sequences of downstream (acceptor) S regions. In the current study, we identify the histone methyltransferase Suv39h1 as a novel Salpha-specific factor that specifically increases IgA switching (Smu-Salpha recombination) in a transiently transfected plasmid S substrate, and demonstrate that this effect requires the histone methyltransferase activity of Suv39h1. Additionally, B cells from Suv39h1-deficient mice have an isotype-specific reduction in IgA switching with no effect on the level of germline Ialpha-Calpha transcripts. Taken together, our results suggest that Suv39h1 activity inhibits the activity of a sequence-specific DNA-binding protein that represses switch recombination to IgA.</p>
dc.identifier.submissionpathwfc_pp/171
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.source.pages1179-88


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