MucA is a small peptide encoded by an overlapping sequence with cdsA that upregulates the biosynthesis of glycolipid MPIase in the cold.

Autor: Hikage R; The United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, Japan., Tadika Y; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate, Japan., Asanuma H; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate, Japan., Han Y; The United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, Japan., Nishiyama KI; The United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, Japan; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate, Japan. Electronic address: nishiyam@iwate-u.ac.jp.
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Aug 20; Vol. 721, pp. 150148. Date of Electronic Publication: 2024 May 20.
DOI: 10.1016/j.bbrc.2024.150148
Abstrakt: MPIase is a glycolipid involved in protein insertion into and preprotein translocation across the cytoplasmic membranes of E. coli. MPIase is upregulated in the cold conditions to overcome the cold-sensitive protein export. CdsA, a CDP-diacylglycerol synthase, catalyzes the first reaction in MPIase biosynthesis. An open reading frame for a peptide of 50 amino acids is encoded immediately after ispU, a neighboring upstream gene of cdsA, and overlaps cdsA to a large extent. Mutational analysis revealed that the expression of this peptide is essential for upregulation of MPIase in the cold. Consistently, expression of this peptide in trans resulted in cold upregulation of MPIase. We therefore named this peptide MucA after its function (MPIase upregulation in the cold). When the partially purified MucA was added to the reaction of the intermediate in MPIase biosynthesis, a significant increase in the product formation was observed, supporting the function of MucA. The possible role of MucA in MPIase biosynthesis is discussed.
Competing Interests: Declaration of competing interest The authors declare that they have no conflicts of interest with regard to the content of this article.
(Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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