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Five structural genes required for ceramide synthesis in Caulobacter and for bacterial survival
Author(s) -
OleaOzuna Roberto Jhonatan,
Poggio Sebastian,
QuirozRocha Elva,
GarcíaSoriano Daniela A.,
SahoneroCanavesi Diana X.,
PadillaGómez Jonathan,
MartínezAguilar Lourdes,
LópezLara Isabel M.,
ThomasOates Jane,
Geiger Otto
Publication year - 2021
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.15280
Subject(s) - caulobacter crescentus , biology , sphingolipid , mutant , gene , microbiology and biotechnology , genetics , biochemistry , cell cycle
Summary Sphingolipids are essential and common membrane components in eukaryotic organisms, participating in many important cellular functions. Only a few bacteria are thought to harbour sphingolipids in their membranes, among them the well‐studied α‐proteobacterium Caulobacter crescentus , a model organism for asymmetric cell division and cellular differentiation. Here, we report that C. crescentus wild type produces several molecular species of dihydroceramides, which are not produced in a mutant lacking the structural gene for serine palmitoyltransferase ( spt ). Whereas growth of a spt ‐deficient mutant and wild type are indistinguishable during the exponential phase of growth, survival of the spt ‐deficient mutant is much reduced, in comparison with wild type, during stationary phase of growth, especially at elevated temperatures. The structural gene for spt is located within a genomic cluster, comprising another 16 genes and which, like spt , are important for fitness of C. crescentus . Mutants deficient in genes linked to spt by high cofitness were unable to produce dihydroceramide or to survive in stationary phase of growth at elevated temperatures. At least five structural genes are required for dihydroceramide biosynthesis in C. crescentus and sphingolipid biosynthesis is needed for survival of this bacterium and the integrity of its outer membrane.