Study on the structure-function of heterochroma chromatin regulatory factor Dbp3-Dbp4
Last Update: 2021-03-05
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chromatin is a carrier of genetic material, usually refers to the linear complex structure of DNA, histones, non-histones, etc. in the nuclei of intercellular cells, which can be divided into normal chromatin and isochromatin. The normal chromatin folding degree is low, in the stretch state, transcription is active, while different chromatin compression is tight and transcription is inactive. Compression of tightly compressed heterochromosomes requires helixing before the fork is copied, followed by DNA replication, and oscic genetic markers (including H3K9me, Histone hypoacetylation) need to be steadily presented to newly synthesized DNA and repack folded. The collaborative completion of these processes is regulated by a range of protein machines. Co-collaborator New York University's Li Fei research team identified protein machines in lysate yeasts, including Cdc20/Pol2, Dpb2, Dpb3 and Dpb4, using protein mass spectrometrometromety. Among them, Cdc20 is the largest catalytic sub-base, mainly responsible for catalytic lead chain synthesis, other sub-base involved in isotrome assembly and silence processes. This study made some progress in the structural function of regulatory factors related toPb3 andPb4.
further genetic studies by the Li Fei research team at New York University have found that Dpb3 and Dpb4 play an important role in the assembly and silence of chromatin and may form interoperable compounds to function. In subsequent biochemistry studies, the Chen Aerospace Research Group of the Institute of Genetics and Developmental Biology of the Chinese Academy of Sciences found that Dpb3 and Dpb4 formed a stable heterogeneic binary complex, further analyzing the high-resolution crystal structure of Dpb3-Dpb4. The structure reveals that Dpb3 and Dpb4 have a histogeneic folding type structure that forms a two-glomeration similar to H2A-H2B. Based on the analysis of three-dimensional structure, it is found that the Dpb3-Dpb4 forms a diglymer complex through extensive interoperability, and proves that the Dpb3-Dpb4 d-cluster structure is essential to play normal function through the study of fixed-point mutation and related functions. In addition, further bio-chemical experiments have found that the compound is interoperable with conservative histone deacetylase, which provides important information for further exploration of its involvement in the assembly and silence of isochromatin.
was published online November 6, 2017 in the journal
(DOI:10.1073/pnas.1712961114). Researcher Chen And Professor Li Fei of New York University are co-authors of the paper, with Dr. He Haijin of the Li Fei Research Group, Dr. Li Yang of the Chen Aerospace Research Group and Dr. Dong Qianhua of the Li Fei Research Group being the co-authors of the paper. The research was supported by the National Major Research and Development Program (2016 YFA0500503), the Strategic Pilot Special Program of the Chinese Academy of Sciences (Category B), and the Natural Science Foundation of China (31470728 and 31728010). (Source: Science.com)
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