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Mouse long-chain acyl-CoA synthetase 1 is active as a monomer
Holly Dykstra1, Chelsea Fisk1, Cassi LaRose1
1Van Andel Institute, Grand Rapids, MI, 49503, USA.
Archives of Biochemistry and Biophysics
|January 24, 2021
Summary
Long-chain acyl-CoA synthetase 1 (ACSL1) activates fatty acids for cellular energy. This study reveals that mouse ACSL1 functions as an active monomer, challenging previous assumptions about its structure.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Metabolism
Background:
- Fatty acids are crucial for cellular structure and energy production.
- Acyl-CoA synthetases (ACSs) activate fatty acids via a thioester linkage with coenzyme A.
- Long-chain acyl-CoA synthetase 1 (ACSL1) is a key enzyme in this process, and its mammalian form is a membrane protein.
Purpose of the Study:
- To characterize the structure and activity of mammalian ACSL1.
- To investigate the oligomeric state of ACSL1 in its active form.
Main Methods:
- Purification of full-length mouse ACSL1.
- Reconstitution of ACSL1 into lipid nanodiscs.
- Enzymatic assays, mutational analysis, and cryo-electron microscopy.
Main Results:
- Mouse ACSL1 was successfully purified and reconstituted.
- Structural and enzymatic data indicate ACSL1 functions as a monomer.
- This contrasts with some previously studied bacterial homologues.
Conclusions:
- Mammalian ACSL1 functions as an active monomer.
- This finding clarifies the oligomeric state of a critical fatty acid activating enzyme.
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