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    Home > Biochemistry News > Biotechnology News > The first experiment proved the new form of dipolymer binding of the transcription factor FOXA1 protein.

    The first experiment proved the new form of dipolymer binding of the transcription factor FOXA1 protein.

    • Last Update: 2020-08-10
    • Source: Internet
    • Author: User
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    Recently, the first experiment of the Ralf Jauch Research Group of the Guangzhou Institute of Biomedicine and Health of the Chinese Academy of Sciences proved the new form of dipolymer binding of the transcription factor FOXA1 protein, and made new progress in the study of the dipolymer effect, which was published online in the journal Nucleic AcidS Research.
    transcription factor protein FOXA1 belongs to one of the members of the forkhead family and plays an important role in the process of cell proliferation, differentiation, embryo growth, organ development, tumor generation and development.
    the expression of FOXA1 protein in tumor cells is highly related to tumor malignancy and molecular disheacity.
    genome sequencing results show that FOXA1 regulates the binding of hormone receptor proteins, such as estrogen receptor proteins (Estrogen Receptor, ER), androgen receptor proteins (Androgen Receptor, AR), glucocorticoid receptor proteins (Glucoticoid Receptor, GR) and other regulatory sinies and downstream genes.
    more specifically, the FOXA1 protein has been shown to bind to nuclear small bodies and to help open closed chromatin structures and allow other transcription factors to bind to corresponding sites, because of its properties, FOXA1 is also known as the "pioneer transcription factor", and studying how FOXA1 identifies and binds the genome has also become an important direction for the study of pioneer transcription factor family proteins.
    Ralf Jauch has long been working on the molecular mechanisms of the regulation of transcription factor proteins and genomic binding. In the early study of the
    , the research group obtained a new batch of transcription factor dipolymer junction sites including FOXA1 ihopolymer binding sites, followed by further research around FOXA1 isopolymer base sequence.
    the study first used biochemical techniques to verify that FOXA1 proteins can be combined in the new base sequence in the form of dipolymers, protein structure simulation showed that the dipolymer binding of FOXA1 protein molecules was mediated by DNA base sequence, and genomic sequencing results showed that FOXA1 foxA1 protein seiswelled in dipolymer base sequence in breast and liver cancer cells and was able to enrich and be able to be able to in PI33 The K signal path regulates the dynamic changes of chromatin when it is inhibited, and secondly, through bioinformatics and cell biology techniques, the single nucleotide polymorphism (SNP) that can affect FOXA1 dipolymer binding, which has the disease-causing SNPs associated with osteoporosis and Parkinson's disease, provides a new direction for future research and treatment of related diseases. the first author of the
    the son is Ph.D. student Wang Xuecheng and the communication author is researcher Ralf Jauch, who has received strong support from collaborators such as the Singapore Institute of Genetics, the University of Warsaw in Poland, the MIT-Harvard-Broad Institute, and the Map Institute in Germany.
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