Open AccessElectrophoretic analysis of DNA‐binding proteins during induction of 3α,20β‐ and 3β,17β‐hydroxysteroid dehydrogenase in wild type and mutants of Streptomyces hydrogenans
Author(s) -
Feller Klaus,
Träger Lothar
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02539.x
Subject(s) - dna , mutant , biochemistry , biology , dehydrogenase , microbiology and biotechnology , hydroxysteroid dehydrogenase , electrophoretic mobility shift assay , wild type , binding protein , dna binding protein , enzyme , gene expression , gene , transcription factor
Abstract Treatment of the wild‐type strain HY 0 of Streptomyces hydrogenans with estradiol, a specific inducer of 3β,17β‐hydroxysteroid dehydrogenase (17β‐HSD) formation, caused several soluble proteins to bind to DNA‐cellulose with altered affinity. Hydrocortisone which induces biosynthesis of 3α,20β‐hydroxysteroid dehydrogenase (20β‐HSD), and progesterone which induces production of both 17β‐ and 20β‐HSD, had no effect on DNA‐binding properties of the proteins. In mutants with altered activity/inducibility of 17β‐ and 20β‐HSD only one DNA‐binding protein (protein 23) still showed an altered DNA affinity in response to estradiol‐treatment and this in only one strain. In other mutants the DNA affinity was not altered during induction with estradiol but the DNA affinity of protein 23 varied between low, low‐and‐high, and high affinity, depending on the strain. In the mutant where DNA affinity was altered by estradiol treatment the change was opposite to that found in the wild type.