Journal of Iwate Medical Assiociation
Online ISSN : 2434-0855
Print ISSN : 0021-3284
Original
Mass spectrometric analysis of erythroid specific 5-aminolevulinate synthase protein complex
Ko SuzukiCostantine Chasama KamataKazumichi Furuyama
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JOURNAL OPEN ACCESS

2023 Volume 75 Issue 2 Pages 69-79

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Abstract

Erythroid-specific 5-aminolevulinate synthase (ALAS2) is the rate-limiting enzyme of the heme biosynthetic pathway in erythroblasts. ALAS2 is essential for supplying heme to produce hemoglobin in developing erythroblasts. While it has been reported that the gene expression of ALAS2 is regulated at the transcriptional and the translational steps, the post-translational regulation of ALAS2 protein is not well understood. In this study, we examined the protein complex of FLAG-tagged ALAS2 (ALAS2F) using immunoprecipitation followed by mass spectrometry and identified several mitochondrial proteins in the complex of ALAS2F. We also confirmed the presence of these proteins in the complex of ALAS2F by Western blot analysis, and we speculated on the novel role of one of these identified proteins on the post-translational regulation of ALAS2 protein. Further studies on the role of these proteins in the regulation of ALAS2 protein will reveal the precise mechanisms of the post-translational regulation of ALAS2 in erythroid cells.

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© 2023 Iwate Medical Association
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