Post-translational modification of erythroid-specific 5-aminolevulinate synthase and its' role in erythroid differentiation.

点击翻译按钮获取中文摘要

Erythroid-specific 5-aminolevulinate synthase (ALAS2) is the rate-limiting enzyme of heme biosynthetic pathway in erythroid cells. In this project, we have tried to clarify how the expression of ALAS2 is regulated post-translationally in vivo. As a result, we found that ALAS2 formed covalent homo-dimer, which was not able to translocate into mitochondria, depending on the concentration of intracellular heme level in HEK293 cells. Moreover, we have identified that ALAS2 protein could be SUMOylated, when it was co-expressed with E1, E2 enzyme of SUMOylation and SUMO1 (Small Ubiquitin like Modifier 1) in E. coli. These post-translational modifications of ALAS2 protein were hitherto unknown phenomena, thus it should be important to examine how these modifications were involved in the functional regulation of ALAS2 protein, as well as in erythroid differentiation.