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Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c‐fos serum response element.
Author(s) -
Schröter H.,
Mueller C.G.,
Meese K.,
Nordheim A.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb08218.x
Subject(s) - biology , glycoprotein , serum response element , ternary complex , microbiology and biotechnology , biochemistry , serum response factor , gene , gene expression , enzyme
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.