Nucleic Acids Research, 1990, Vol. 18, No. 19 5713-5716
© 1990
MOLECULAR BIOLOGY |
A single-stranded DNA-binding protein promotes the binding of the purified oestrogen receptor to its responsive element
Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Unité 184 de Biologie Moléculaire et de Génie Génétique de I'INSERM, Institut de Chimie Biologique Faculté de Médecine, 11 Rue Humann, 67085 Strasbourg Cédex, France
*To whom correspondence should be addressed
Received July 4, 1990. Revised September 3, 1990. Accepted September 3, 1990.
The purified human oestrogen receptor (hER) does not form a detectable complex with an oestrogen responsive element (ERE) under conditions where hER-ERE complexes are readily formed with crude extracts from Hela or yeast cells expressing the hER. This Indicates that other factor(s) are necessary for ER-ERE binding. Such a ER DNA binding stimulatory factor (DBSF) has been purified from the yeast Saccharomyces cerevislae. It is a 45 kDa single-stranded DNA-binding protein (SSB) which cannot be substituted for by the purified E.coi SSB.
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