RRC ID 81112
Author Nishikawa A, Karita S, Umekawa M.
Title Ngk1 kinase-mediated N-acetylglucosamine metabolism promotes UDP-GlcNAc biosynthesis in Saccharomyces cerevisiae.
Journal FEBS Lett
Abstract N-acetylglucosamine (GlcNAc) is an important structural component of the cell wall chitin, N-glycans, glycolipids, and GPI-anchors in eukaryotes. GlcNAc kinase phosphorylates GlcNAc into GlcNAc-6-phosphate, a precursor of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) that serves as a substrate for glycan synthesis. Although GlcNAc kinase is found widely in organisms ranging from microorganisms to mammals, it has never been found in the model yeast Saccharomyces cerevisiae. Here, we demonstrate the presence of GlcNAc metabolism for UDP-GlcNAc biosynthesis in S. cerevisiae through Ngk1, a GlcNAc kinase we discovered previously. The overexpression or deletion of Ngk1 in the presence of GlcNAc affected the amount of both UDP-GlcNAc and chitin, suggesting that GlcNAc metabolism via Ngk1 promotes UDP-GlcNAc synthesis. Our data suggest that the Ngk1-mediated GlcNAc metabolism compensates for the hexosamine pathway, a known pathway for UDP-GlcNAc synthesis.
Volume 598(13)
Pages 1644-1654
Published 2024-7-1
DOI 10.1002/1873-3468.14881
PMID 38622055
MeSH Acetylglucosamine* / metabolism Chitin / biosynthesis Chitin / metabolism Phosphorylation Phosphotransferases (Alcohol Group Acceptor)* / genetics Phosphotransferases (Alcohol Group Acceptor)* / metabolism Saccharomyces cerevisiae* / genetics Saccharomyces cerevisiae* / metabolism Saccharomyces cerevisiae Proteins* / genetics Saccharomyces cerevisiae Proteins* / metabolism Uridine Diphosphate N-Acetylglucosamine* / metabolism
Resource
DNA material Genomic DNA of Candida albicans JCM 1542 T (JGD07967)