The identification mechanism of SHL protein for inhibition and active histone modification.

On June 21st, the journal Nature Communications published online the Dual recognition of The Dual recognition of H3K4me3 and H3K27me3 by the Dujiamu Research Group of the Plant Molecular Genetics National Key Laboratory of the Plant Adverse Biology Research Center of the Institute of Plant Biology of the Chinese Academy of Sciences. A plant histone reader SHL research paper, the use of structural biology, biochemistry, plant molecular genetics and genomics and other means to jointly reveal the plant-specific histone recognition protein SHL through its own BAH domain and PHD domain to identify inhibitory histone modification H3K27me3 and active histone modification H3K4me3 molecular mechanisms.
histone transcribe modification, as one of the important regulatory mechanisms in epigenetics, plays an important role in a variety of biological processes, including gene expression regulation.
histone modification recognition factors have the ability to identify specificities for different histone modifications, and play an important role in the state regulation of chromosomes.
usually identify proteins that contain multiple histone-identifying domains, which are usually present in series and work in multivalent chromatin binding.
short LIFE (SHL) has two potential histone recognition factors at the same time: BAH and PHD domain, which play an important regulatory role in the flowering of the amoeba and the dormant of seeds.
previous reports have shown that SHL can inhibit flowering by inhibiting the expression of the integration factor OFSUPPRESSOVEREXPRESSION OF CO1 (SOC1) during flowering.
Although the SHL protein plays a role in inhibiting flowering, its specific molecular mechanism is not yet clear.
the study, the researchers first found that SHL proteins can identify histone activation modified H3K4me3 and histone inhibition modification H3K27me3, and itwasy with ITC confirmed that SHL can identify methylated H3K4 and H3K27.
followed by X-ray crystal diffraction, the researchers analyzed the composite structures of SHL with H3K4me3 and H3K27me3 respectively, and combined with other biochemical experiments, confirmed that SHL was able to independently identify active histone marker sepsis H3K4me3 and inhibited marker H3K27me3 through its PHD and BAH domains, respectively.
the Chip-seq experiment confirmed that SHL distribution in the body was associated with areas of co-enrichment H3K4me3 and H3K27me3.
genetic experiments have shown that the combination site mutations of BAH-H3K27me3 and PHD-H3K4me3 in SHL proteins can not be refilled with the early shl mutant flowering phenotype, indicating that the combination of SHL and H3K27me3 and H3K4me3 has important functionin in the body. Lu Weichen, a second-year graduate student at the
Adversity Center, is the co-first author of the round, and Du Jiamu and Zhong Snowflake are co-authors.
bl19U1 (SSRF), a national protein facility for the shanghai synchrotron radiation source, provides timely and effective support for data collection.
the research work has been funded by the Ministry of Science and Technology's National Key Research and Development Program, the National Natural Science Foundation of China and the Chinese Academy of Sciences.
.