Coordinated upregulation of two CDP-diacylglycerol synthases, YnbB and CdsA, is essential for cell growth and membrane protein export in the cold.

Autor:	Kamemoto Y; The United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate 020-8550, Japan., Hikage R; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate 020-8550, Japan., Han Y; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate 020-8550, Japan., Sekiya Y; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate 020-8550, Japan., Sawasato K; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate 020-8550, Japan., Nishiyama KI; The United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate 020-8550, Japan.; Department of Applied Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate 020-8550, Japan.
Jazyk:	angličtina
Zdroj:	FEMS microbiology letters [FEMS Microbiol Lett] 2023 Jan 17; Vol. 370.
DOI:	10.1093/femsle/fnad131
Abstrakt:	YnbB is a paralogue of CdsA, a CDP-diacylglycerol synthase. While the cdsA gene is essential, the ynbB gene is dispensable. So far, no phenotype of ynbB knockout has been observed. We found that a ynbB knockout strain acquired cold-sensitivity on growth under CdsA-limited conditions. We found that MPIase, a glycolipid involved in protein export, is cold-upregulated to facilitate protein export in the cold, by increasing the mRNA levels of not only CdsA but also that of YnbB. Under non-permissive conditions, phospholipid biosynthesis proceeded normally, however, MPIase upregulation was inhibited with accumulation of precursors of membrane and secretory proteins such as M13 procoat and proOmpA, indicating that YnbB is dedicated to MPIase biosynthesis, complementing the CdsA function. (© The Author(s) 2023. Published by Oxford University Press on behalf of FEMS.)
Databáze:	MEDLINE
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