98%
921
2 minutes
20
Mixed-linkage (1,3;1,4)-β-glucan (MLG), an abundant cell wall polysaccharide in the Poaceae, has been detected in ascomycetes, algae, and seedless vascular plants, but not in eudicots. Although MLG has not been reported in bryophytes, a predicted glycosyltransferase from the moss (Pp3c12_24670) is similar to a bona fide ascomycete MLG synthase. We tested whether encodes an MLG synthase by expressing it in wild tobacco () and testing for release of diagnostic oligosaccharides from the cell walls by either lichenase or (1,4)-β-glucan endohydrolase. Lichenase, an MLG-specific endohydrolase, showed no activity against cell walls from transformed , but (1,4)-β-glucan endohydrolase released oligosaccharides that were distinct from oligosaccharides released from MLG by this enzyme. Further analysis revealed that these oligosaccharides were derived from a novel unbranched, unsubstituted arabinoglucan (AGlc) polysaccharide. We identified sequences similar to the AGlc synthase from algae, bryophytes, lycophytes, and monilophytes, raising the possibility that other early divergent plants synthesize AGlc. Similarity of AGlc synthase to MLG synthases from ascomycetes, but not those from Poaceae, suggests that AGlc and MLG have a common evolutionary history that includes loss in seed plants, followed by a more recent independent origin of MLG within the monocots.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6048786 | PMC |
http://dx.doi.org/10.1105/tpc.18.00082 | DOI Listing |
Plant J
July 2025
Biology Department, University of Massachusetts, Amherst, Massachusetts, 01003, USA.
Cellulose is synthesized at the plasma membrane by the cellulose synthase complex, a structure that contains three distinct isoforms of the catalytic subunit, cellulose synthase A (CESA). The division into three subunits appears early in land plant evolution and is highly conserved, particularly for the secondary cell wall. However, what if any unique roles each isoform plays in the complex remain unclear.
View Article and Find Full Text PDFPlant Mol Biol
July 2025
Department of Biological Sciences, University of Rhode Island, Kingston, RI, 02881, USA.
The fundamental mechanism of cellulose synthesis is widely conserved across Kingdoms and depends on cellulose synthases, which are processive, dual-function, family 2 glycosyltransferases (GT-2). These enzymes polymerize glucose on the cytoplasmic side of the plasma membrane and export the glucan chain to the cell surface through an integral transmembrane (TM) channel. Structural studies of active plant cellulose synthases (CESAs) have revealed interactions between the nascent glucan chain and the side chains of polar, charged, and aromatic amino acid residues that line the TM channel.
View Article and Find Full Text PDFPlant J
July 2025
Pharmaceutical Institute, Department of Pharmaceutical Biology, Christian-Albrechts-University of Kiel, Gutenbergstraße 76, 24118, Kiel, Germany.
Two bryophyte models, the hornwort Anthoceros agrestis (Anthoceros) and the moss Physcomitrium patens (Physcomitrium), were analyzed for the presence of arabinogalactan-proteins (AGPs), as the emergence of these signaling glycoproteins in evolution is still under debate. AGPs of both species had a galactan core structure similar to that of other bryophyte and fern AGPs, but different from angiosperm AGPs, as 1,6-linked pyranosidic galactose was almost absent. In the Physcomitrium AGP, furanosidic arabinose (Araf) linkages were mainly terminal (10%) or 5-linked (13%), while in Anthoceros, terminal Araf dominated (26%) and was accompanied by very low amounts of 1,3-Araf and pyranosidic terminal Ara.
View Article and Find Full Text PDFSci Adv
December 2024
Department of Biological Sciences, University of Rhode Island, Kingston, RI 02881, USA.
Similar to cellulose synthases (CESAs), cellulose synthase-like D (CSLD) proteins synthesize β-1,4-glucan in plants. CSLDs are important for tip growth and cytokinesis, but it was unknown whether they form membrane complexes in vivo or produce microfibrillar cellulose. We produced viable CESA-deficient mutants of the moss to investigate CSLD function without interfering CESA activity.
View Article and Find Full Text PDFMatrix Biol
April 2023
Department of Pathology and Genomic Medicine and the Translational Cellular Oncology Program, Sidney Kimmel Cancer Center, Sidney Kimmel Medical College at Thomas Jefferson University, Philadelphia, PA 19107, USA. Electronic address:
The tumor stroma of most solid malignancies is characterized by a pathological accumulation of pro-angiogenic and pro-tumorigenic hyaluronan driving tumorigenesis and metastatic potential. Of all three hyaluronan synthase isoforms, HAS2 is the primary enzyme that promotes the build-up of tumorigenic HA in breast cancer. Previously, we discovered that endorepellin, the angiostatic C-terminal fragment of perlecan, evokes a catabolic mechanism targeting endothelial HAS2 and hyaluronan via autophagic induction.
View Article and Find Full Text PDF