Kathryn A. Piffat , Radmila Hrdličková , Jiri Nehyba , Toshio Ikeda , Andrew Liss , Sidong Huang , Saı̈d Sif , Thomas D. Gilmore , Henry R. Bose Jr.
{"title":"鸡RelB转录因子具有不同于哺乳动物RelB的转录激活序列和组织特异性表达模式","authors":"Kathryn A. Piffat , Radmila Hrdličková , Jiri Nehyba , Toshio Ikeda , Andrew Liss , Sidong Huang , Saı̈d Sif , Thomas D. Gilmore , Henry R. Bose Jr.","doi":"10.1006/mcbr.2001.0290","DOIUrl":null,"url":null,"abstract":"<div><p>Rel/NF-κB proteins are eukaryotic transcription factors that control the expression of genes involved in a large variety of cellular processes. Rel proteins share a highly conserved DNA-binding/dimerization domain called the Rel Homology (RH) domain. We have constructed and characterized a composite cDNA encoding most of the chicken RelB transcription factor. The predicted chicken RelB protein has a high degree of sequence similarity to other vertebrate RelB proteins within the RH domain, but is much less conserved outside this domain. Chicken RelB does not bind DNA as a homodimer, but forms DNA-binding heterodimers with NF-κB p50 or p52. Overexpressed chicken RelB localizes to the nucleus in chicken embryo fibroblasts, and the nonconserved C-terminal sequences of chicken RelB contain a transactivation domain that functions in chicken and mouse fibroblasts. Thus, chicken RelB has functional properties similar to other vertebrate RelB proteins. However, Western blotting of diverse chicken tissues indicates that chicken RelB is more widely expressed than mammalian RelB.</p></div>","PeriodicalId":80086,"journal":{"name":"Molecular cell biology research communications : MCBRC","volume":"4 5","pages":"Pages 266-275"},"PeriodicalIF":0.0000,"publicationDate":"2001-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/mcbr.2001.0290","citationCount":"1","resultStr":"{\"title\":\"The Chicken RelB Transcription Factor Has Transactivation Sequences and a Tissue-Specific Expression Pattern That Are Distinct from Mammalian RelB\",\"authors\":\"Kathryn A. Piffat , Radmila Hrdličková , Jiri Nehyba , Toshio Ikeda , Andrew Liss , Sidong Huang , Saı̈d Sif , Thomas D. Gilmore , Henry R. Bose Jr.\",\"doi\":\"10.1006/mcbr.2001.0290\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Rel/NF-κB proteins are eukaryotic transcription factors that control the expression of genes involved in a large variety of cellular processes. Rel proteins share a highly conserved DNA-binding/dimerization domain called the Rel Homology (RH) domain. We have constructed and characterized a composite cDNA encoding most of the chicken RelB transcription factor. The predicted chicken RelB protein has a high degree of sequence similarity to other vertebrate RelB proteins within the RH domain, but is much less conserved outside this domain. Chicken RelB does not bind DNA as a homodimer, but forms DNA-binding heterodimers with NF-κB p50 or p52. Overexpressed chicken RelB localizes to the nucleus in chicken embryo fibroblasts, and the nonconserved C-terminal sequences of chicken RelB contain a transactivation domain that functions in chicken and mouse fibroblasts. Thus, chicken RelB has functional properties similar to other vertebrate RelB proteins. However, Western blotting of diverse chicken tissues indicates that chicken RelB is more widely expressed than mammalian RelB.</p></div>\",\"PeriodicalId\":80086,\"journal\":{\"name\":\"Molecular cell biology research communications : MCBRC\",\"volume\":\"4 5\",\"pages\":\"Pages 266-275\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2001-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1006/mcbr.2001.0290\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular cell biology research communications : MCBRC\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1522472401902909\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular cell biology research communications : MCBRC","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1522472401902909","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The Chicken RelB Transcription Factor Has Transactivation Sequences and a Tissue-Specific Expression Pattern That Are Distinct from Mammalian RelB
Rel/NF-κB proteins are eukaryotic transcription factors that control the expression of genes involved in a large variety of cellular processes. Rel proteins share a highly conserved DNA-binding/dimerization domain called the Rel Homology (RH) domain. We have constructed and characterized a composite cDNA encoding most of the chicken RelB transcription factor. The predicted chicken RelB protein has a high degree of sequence similarity to other vertebrate RelB proteins within the RH domain, but is much less conserved outside this domain. Chicken RelB does not bind DNA as a homodimer, but forms DNA-binding heterodimers with NF-κB p50 or p52. Overexpressed chicken RelB localizes to the nucleus in chicken embryo fibroblasts, and the nonconserved C-terminal sequences of chicken RelB contain a transactivation domain that functions in chicken and mouse fibroblasts. Thus, chicken RelB has functional properties similar to other vertebrate RelB proteins. However, Western blotting of diverse chicken tissues indicates that chicken RelB is more widely expressed than mammalian RelB.