Metabolic regulation via protein acylation in Thermus thermophilus

2015 Fiscal Year Final Research Report

• Project/Area Number: 26870113
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Applied biochemistry; Applied microbiology
• Research Institution: The University of Tokyo
• Principal Investigator: Yoshida Ayako 東京大学, 生物生産工学研究センター, 特任助教 (90633686)
• Co-Investigator(Renkei-kenkyūsha): KOSONO Saori 東京大学, 生物生産工学研究センター, 特任准教授 (90321760) ; NISHIYAMA Makoto 東京大学, 生物生産工学研究センター, 教授 (00208240)
• Project Period (FY): 2014-04-01 – 2016-03-31
• Keywords: タンパク質アシル化修飾 / タンパク質アセチル化酵素 / アミノ酸代謝 / CoA体代謝 / 代謝調節 / タンパク質間相互作用

Outline of Final Research Achievements

The proteomic analysis revealed that a lot of proteins were acetylated and succinylated in Thermus thermophilus HB27. 2-isopropylmalate synthase (IPMS), which catalyzes the first step of leucine biosynthesis, is both acetylated and succinylated. The acylation-mimic mutant showed the lower activity and changed the substrate specificity. We suppose that the acylation on IPMS may regulate the flux of branched-chain amino acids.
The analysis of protein lysine acetyltransferase (KAT) from T. thermophilus identified the CoA transferase as an acetylation substrate of KAT. Since this CoA transferase uses Acetyl-CoA, which is a substrate of KAT, suggesting that the acetylation of CoA transferase regulates CoA metabolism depending on the concentration of Acetyl-CoA. Moreover, we found the protein interacting with this CoA transferase, suggesting that the activity of CoA transferase is regulated in a complex manner including protein acylation and regulatory protein binding.

Free Research Field

応用微生物学