Identification of acylhomoserine lactone synthases by affinity beads
Project/Area Number |
26450140
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Bioorganic chemistry
|
Research Institution | Osaka Prefecture University |
Principal Investigator |
Kai Kenji 大阪府立大学, 生命環境科学研究科, 講師 (40508404)
|
Project Period (FY) |
2014-04-01 – 2017-03-31
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
Keywords | クオラムセンシング / アシルホモセリンラクトン / ケミカルバイオロジー / アフィニティービーズ / AHL合成酵素 / プルダウン |
Outline of Final Research Achievements |
Bacteria communicate using chemical signals to sense cell density and regulate diverse coordinated behaviors by a process known as quorum sensing (QS). N-Acylhomoserine lactones (AHLs), one class of QS signals in Gram-negative bacteria, are synthesized from the acyl-acyl carrier protein (acyl-ACP) and S-adenosylmethionine (SAM) by LuxI-type synthases. We here report the affinity purification of AHL synthases using beads conjugated with an enzyme inhibitor, which was designed based on the catalytic intermediate acyl-SAM. This is the first study to show that QS signal synthases could be purified by a ligand-based affinity protocol.
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Report
(4 results)
Research Products
(4 results)