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• W207200575 abstract "Research Article1 April 1990free access Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element. H. Schröter H. Schröter Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author C.G. Mueller C.G. Mueller Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author K. Meese K. Meese Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author A. Nordheim A. Nordheim Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author H. Schröter H. Schröter Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author C.G. Mueller C.G. Mueller Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author K. Meese K. Meese Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author A. Nordheim A. Nordheim Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. Search for more papers by this author Author Information H. Schröter1, C.G. Mueller1, K. Meese1 and A. Nordheim1 1Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG. The EMBO Journal (1990)9:1123-1130https://doi.org/10.1002/j.1460-2075.1990.tb08218.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Transcriptional regulation of the c-fos proto-oncogene requires the serum response element (SRE) which is complexed by a multi-protein assembly observed both in vitro and in vivo. Two protein factors, p67SRF and p62TCF (previously called p62), are required to interact with the SRE for efficient induction of c-fos by serum. By quantitative band shift electrophoresis we measure at least a 50-fold increase in SRE affinity for p67SRF/p62TCF over p67SRF alone. Stoichiometrically we determine that the ternary complex with p62TCF involves p67SRF in dimeric form. We demonstrate that p67SRF is a glycosylated nuclear transcription factor carrying terminal N-acetylglucosamine (GlcNAc) as a post-translational modification. A proteolytic limit digestion product, approximately 13 kd in size, was generated from the p67SRF-SRE complex. This p67SRF-core domain binds SRE, can dimerize with p67SRF and is still able to form a ternary complex with p62TCF. Therefore, three functional activities can be ascribed to this small p67SRF-core domain: specific DNA binding, dimerization and interaction with p62TCF. We demonstrate that these functions map within the p67SRF core fragment containing the region between amino acids 93 and 222. Previous ArticleNext Article Volume 9Issue 41 April 1990In this issue RelatedDetailsLoading ..." @default.
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• W207200575 title "Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element." @default.
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