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Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants
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Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants
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Journal Article
Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants
2019
Overview
Mannans are an abundant cell wall polysaccharide in bryophytes, seedless vascular plants and gymnosperms. A previous study has shown that mannan acetylation in Arabidopsis and konjac is mediated by mannan O-acetyltransferases belonging to the Domain of Unknown Function (DUF) 231 family. However, little is known about the acetylation patterns of mannans in bryophytes and seedless vascular plants, and the evolutionary origin of mannan O-acetyltransferases in land plants has not yet been studied.
Phylogenetic analysis of the DUF231 family revealed that DUF231 members were present in the charophycean green algae and evolved to form overlapped and divergent phylogenetic groups in different taxa of land plants.
Acetyltransferase activity assays of recombinant proteins demonstrated that a number of group II DUF231 members from moss, Selaginella, pine, spruce, rice and poplar were mannan 2-O- and 3-O-acetyltransferases, whereas the two group I DUF231 members from the alga Klebsormidium nitens were not. Structural analysis of mannans from moss and Selaginella showed they were composed of mannosyl and glucosyl residues and the mannosyl residues were acetylated at O-2 and O-3.
These findings indicate that although the DUF231 genes originated in algae, their recruitment as mannan O-acetyltransferases probably occurred in bryophytes, and the biochemical functions of these O-acetyltransferases are evolutionarily conserved throughout land plants.
Publisher
Wiley,Wiley Subscription Services, Inc,Wiley-Blackwell
Subject
/ Acetyltransferases - genetics
/ Acetyltransferases - metabolism
/ Algae
/ DUF231
/ Genes
/ Humans
/ Mannan
/ Mannans
/ moss
/ Mosses
/ Picea
/ pine
/ Poplar
/ Populus
/ Proton Magnetic Resonance Spectroscopy
/ Recombinant Proteins - biosynthesis
/ Residues
/ rice
/ spruce
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