Thinking outside the CaaX-box: an unusual reversible prenylation on ALDH9A1

Author:

Suazo Kiall F.1ORCID,Bělíček Jakub2ORCID,Schey Garrett L.3ORCID,Auger Shelby A.1ORCID,Petre Alexandru M.1ORCID,Li Ling4ORCID,Błażewska Katarzyna M.5ORCID,Kopečný David2ORCID,Distefano Mark D.1ORCID

Affiliation:

1. Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA

2. Department of Experimental Biology, Faculty of Science, Palacký University, CZ-78371, Czech Republic

3. Department of Medicinal Chemistry, University of Minnesota, Minneapolis, MN 55455, USA

4. Department of Experimental and Clinical Pharmacology, University of Minnesota, Minneapolis, MN, 55455, USA

5. Institute of Organic Chemistry, Faculty of Chemistry, Lodz University of Technology, Łódź, Poland

Abstract

Protein prenylation typically involves linkage of the lipid via a thioether bond. Here we report the discovery of prenoylation, a thioester-linked modification. In the case of ALDH9A1, this modification may serve an important regulatory function.

Funder

National Institute of General Medical Sciences

National Institute on Aging

Narodowe Centrum Nauki

Univerzita Palackého v Olomouci

Ministerstvo Školství, Mládeže a Tělovýchovy

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

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