Deinococcus radiodurans, although a gram-positive bacterium, has a complex cell wall with multiple layers and associates to this structural particularity, a quite unusual lipid composition for gram-positive bacteria. The conventional phospholipids (phosphatidyl ethanolamine, phosphatidyl choline, phosphatidyl glycerol...) are absent. Among the nine polar lipids detected in the R1 Anderson strain, three are glycolipids only one is a phospholipid, the other ones are glycophospholipids. One of the latter compounds contains one free amino group. Analysis by aminoacid autoanalyser enables to identify glucosamine in one glycolipid and in two glycophospholipids. Sugar analysis by gas-liquid chromatography after acid methanolysis and trifluoroacetylation, reveals the occurrence of N-acetyl glucosaminyl residues in one glycolipid and in one phospholipid. The following identification for the two lipids of D. radiodurans is proposed: phosphatidyl glucosaminyl glycerol and phosphatidyl N-acetyl glucosaminyl glycerol.
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http://dx.doi.org/10.1016/0300-9084(84)90009-9 | DOI Listing |
Anal Chem
January 2025
Molecular and Cellular Biology Graduate Program, University of Massachusetts, Amherst, Massachusetts 01003, United States.
Matrix-assisted laser desorption ionization mass spectrometry imaging (MALDI-MSI) has been used to generate spatial maps of lipids, metabolites, peptides, proteins, and glycans in tissues; however, its use for mapping extracellular matrix (ECM) protein distributions is underexplored. ECM proteins play a major role in various pathological conditions, and changes in their spatial distributions affect the function and morphology of cells within tissues. ECM protein detection is challenging because they are large, insoluble, and undergo various post-translational modifications, such as glycosylation.
View Article and Find Full Text PDFAnal Chem
December 2024
Department of Pathology, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21231, United States.
Glycobiology
September 2024
Glycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research (CPR), Riken, 2-1 Hirosawa, Wako Saitama 351-0198, Japan.
Cytosolic peptide: N-glycanase (PNGase/NGLY1 in mammals) is an amidase (EC:3.5.1.
View Article and Find Full Text PDFFEBS Lett
September 2024
Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Japan.
JCI Insight
October 2024
Horae Gene Therapy Center, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
The cytoplasmic peptide:N-glycanase (NGLY1) is ubiquitously expressed and functions as a de-N-glycosylating enzyme that degrades misfolded N-glycosylated proteins. NGLY1 deficiency due to biallelic loss-of-function NGLY1 variants is an ultrarare autosomal recessive deglycosylation disorder with multisystemic involvement; the neurological manifestations represent the main disease burden. Currently, there is no treatment for this disease.
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