scholarly journals Interaction of DNA-binding proteins with a milk protein gene promoter in vitro: identification of a mammary gland-specific factor

1991 ◽  
Vol 19 (23) ◽  
pp. 6603-6610 ◽  
Author(s):  
Christine J. Waston ◽  
Katrina E. Gordon ◽  
Morag Robertson ◽  
A. John Clark
2017 ◽  
Vol 39 (8) ◽  
Author(s):  
Farah Deeba ◽  
Tasawar Sultana ◽  
Tariq Mahmood ◽  
Charlotte O’Shea ◽  
Karen Skriver ◽  
...  

1991 ◽  
Vol 11 (7) ◽  
pp. 3745-3755 ◽  
Author(s):  
M Schmitt-Ney ◽  
W Doppler ◽  
R K Ball ◽  
B Groner

Transcription from the beta-casein milk protein gene promoter is induced by the synergistic action of glucocorticoid and prolactin hormones in the murine mammary epithelial cell line, HC11. We analyzed the binding of nuclear proteins to the promoter and determined their binding sites. Site-directed mutagenesis was used to determine the function of nuclear factor binding. During lactogenic hormone induction of HC11 cells, the binding of two nuclear factors increased. The binding of two other nuclear factors, present in uninduced cells, decreased. The basal activity of the promoter could be increased to and above the level of the induced wild-type promoter when the recognition sequences of the negatively regulated factors were mutated. This suggests that the beta-casein promoter is regulated by the relief of the repression of transcription. An essential tissue-specific factor was also found in nuclear extracts from the mammary glands of mice. Mutation of its recognition sequence in the beta-casein promoter led to the abolition of the induction of transcription by lactogenic hormones. The DNA sequences recognized by all five of these nuclear factors are conserved in the promoters of different casein genes from several species, confirming their importance in the regulation of milk protein gene transcription.


1991 ◽  
Vol 11 (7) ◽  
pp. 3745-3755
Author(s):  
M Schmitt-Ney ◽  
W Doppler ◽  
R K Ball ◽  
B Groner

Transcription from the beta-casein milk protein gene promoter is induced by the synergistic action of glucocorticoid and prolactin hormones in the murine mammary epithelial cell line, HC11. We analyzed the binding of nuclear proteins to the promoter and determined their binding sites. Site-directed mutagenesis was used to determine the function of nuclear factor binding. During lactogenic hormone induction of HC11 cells, the binding of two nuclear factors increased. The binding of two other nuclear factors, present in uninduced cells, decreased. The basal activity of the promoter could be increased to and above the level of the induced wild-type promoter when the recognition sequences of the negatively regulated factors were mutated. This suggests that the beta-casein promoter is regulated by the relief of the repression of transcription. An essential tissue-specific factor was also found in nuclear extracts from the mammary glands of mice. Mutation of its recognition sequence in the beta-casein promoter led to the abolition of the induction of transcription by lactogenic hormones. The DNA sequences recognized by all five of these nuclear factors are conserved in the promoters of different casein genes from several species, confirming their importance in the regulation of milk protein gene transcription.


2002 ◽  
Vol 277 (20) ◽  
pp. 17589-17596 ◽  
Author(s):  
Marie Kannius-Janson ◽  
Eva M. Johansson ◽  
Gunnar Bjursell ◽  
Jeanette Nilsson

2004 ◽  
Vol 71 (2) ◽  
pp. 135-140 ◽  
Author(s):  
Paul A Sheehy ◽  
James J Della-Vedova ◽  
Kevin R Nicholas ◽  
Peter C Wynn

A method for the collection of mammary biopsies developed previously was refined and used to study the endocrine regulation of bovine milk protein gene expression. Our surgical biopsy method used real-time ultrasound imaging and epidural analgesia to enable recovery of a sufficient quantity of mammary tissue from late-pregnant dairy cows for explant culture in vitro. The time of biopsy was critical for prolactin-dependent induction of milk protein gene expression in mammary explants, as only mammary tissue from cows nearing 30 d prepartum was hormone-responsive. This suggests that during the later stages of pregnancy a change in the responsiveness of milk protein gene expression to endocrine stimuli occurred in preparation for lactation. This may relate to the diminution of a putative population of undifferentiated cells that were still responsive to prolactin. Alternatively, the metabolic activity of the tissue had increased to the level whereby the response of the tissue was no longer assessable using this model in vitro.


1992 ◽  
Vol 6 (8) ◽  
pp. 1242-1248
Author(s):  
S Ali ◽  
M Edery ◽  
I Pellegrini ◽  
L Lesueur ◽  
J Paly ◽  
...  

2016 ◽  
Author(s):  
Long Qian ◽  
Edo Kussell

AbstractEctopic DNA binding by transcription factors and other DNA binding proteins can be detrimental to cellular functions and ultimately to organismal fitness. The frequency of protein-DNA binding at non-functional sites depends on the global composition of a genome with respect to all possible short motifs, or k-mer words. To determine whether weak yet ubiquitous protein-DNA interactions could exert significant evolutionary pressures on genomes, we correlate in vitro measurements of binding strengths on all 8-mer words from a large collection of transcription factors, in several different species, against their relative genomic frequencies. Our analysis reveals a clear signal of purifying selection to reduce the large number of weak binding sites genome-wide. This evolutionary process, which we call global selection, has a detectable hallmark in that similar words experience similar evolutionary pressure, a consequence of the biophysics of protein-DNA binding. By analyzing a large collection of genomes, we show that global selection exists in all domains of life, and operates through tiny selective steps, maintaining genomic binding landscapes over long evolutionary timescales.


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