On December 10th, researchers such as Stanford University and the University of Texas published an article entitled "SETD3 is an actin histidine methyltransferase that prevents primary dystocia" in Nature. The first mammalian protein was discovered by mouse experiments. Histidine methyltransferase SETD3 and its key regulatory effect on smooth muscle contraction.
It has been found that mammalian actin histidine 73 methylation (actin-H73me) has been in existence for more than 50 years. In addition to mammals, actin-H73me is also present in several other types of plants and animals. Despite the universality of the presence of H73me, the function of this methylation modification and its catalyzed enzymes remain unsolved. In the present study, the researchers identified that SETD3 (SET domain protein 3) is a methyltransferase of physiological actin histidine 73, and further structural analysis revealed that a wide range of interaction networks will actin peptides. The chain "sands" to the surface of SETD3 and correctly positions H73 in the corresponding catalytic domain to facilitate methyl transfer. H73me reduces the nucleotide exchange rate on actin monomers and moderately accelerates the assembly of actin filaments. Mice lacking SETD3 showed complete deletion of actin-H73me in multiple tissues, and quantitative proteomics demonstrated that actin-H73 is the major physiological substrate for SETD3. Female mice lacking SETD3 have a severe reduction in litter size due to dystocia, and this dystocia is also difficult to relieve with oxytocin. In addition, deletion of SETD3 impairs signal-induced contraction of primary human uterine smooth muscle cells. This study found the first mammalian protein histidine methyltransferase on the one hand and the key role of SETD3 and actin-H73me in regulating smooth muscle contraction on the other hand. (Excerpt from Nature, Published: 10 December 2018)
Source: Ministry of Science and Technology
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