ArticleJournal of molecular biology2010
Functional states of homooligomers: insights from the evolution of glycosyltransferases.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 50 citations in OpenAlex.
- Structural variability of multifunctional proteins indicates frequent stochastic evolution of protein oligomers.Communications biology · 2025Article
- Exploring Daptomycin Hypersensitivity inInternational journal of molecular sciences · 2025Article
- Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.The FEBS journal · 2025Article
- Frequent transitions in self-assembly across the evolution of a central metabolic enzyme.Nature communications · 2024Article
- Frequent transitions in self-assembly across the evolution of a central metabolic enzyme.bioRxiv : the preprint server for biology · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Mechanistic insights into glycoside 3-oxidases involved in C-glycoside metabolism in soil microorganisms.Nature communications · 2023Article
- Subfunctionalization of a monolignol to a phytoalexin glucosyltransferase is accompanied by substrate inhibition.Plant communications · 2023Article
- Structure of the human heparan sulfate polymerase complex EXT1-EXT2.Nature communications · 2022Article
- Article
- Deep evolutionary analysis reveals the design principles of fold A glycosyltransferases.eLife · 2020Article
- Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers.Cellular and molecular life sciences : CMLS · 2018Review
- Do Galactolipid Synthases Play a Key Role in the Biogenesis of Chloroplast Membranes of Higher Plants?Frontiers in plant science · 2018Review
- Article
- Calcium/calmodulin alleviates substrate inhibition in a strawberry UDP-glucosyltransferase involved in fruit anthocyanin biosynthesis.BMC plant biology · 2016Article
- Comparative interactions of withanolides and sterols with two members of sterol glycosyltransferases from Withania somnifera.BMC bioinformatics · 2015Article
- Neofunctionalization of the Sec1 α1,2fucosyltransferase paralogue in leporids contributes to glycan polymorphism and resistance to rabbit hemorrhagic disease virus.PLoS pathogens · 2015Article
- Organizational interplay of Golgi N-glycosyltransferases involves organelle microenvironment-dependent transitions between enzyme homo- and heteromers.The Journal of biological chemistry · 2014Article
- Evolutionary diversification of the multimeric states of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Tertiary model of a plant cellulose synthase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Glycosylation is an important aspect of epigenetic regulation. Glycosyltransferase is a key enzyme in the biosynthesis of glycans, which glycosylates more than half of all proteins in eukaryotes and is involved in a wide range of biological processes. It has been suggested previously that homooligomerization in glycosyltransferases and other proteins might be crucial for their function. In this study, we explore functional homooligomeric states of glycosyltransferases in various organisms, trace their evolution, and perform comparative analyses to find structural features that can mediate or disrupt the formation of different homooligomers. First, we make a structure-based classification of the diverse superfamily of glycosyltransferases and confirm that the majority of the structures are indeed clustered into the GT-A or GT-B folds. We find that homooligomeric glycosyltransferases appear to be as ancient as monomeric glycosyltransferases and go back in evolution to the last universal common ancestor (LUCA). Moreover, we show that interface residues have significant bias to be gapped out or unaligned in the monomers, implying that they might represent features crucial for oligomer formation. Structural analysis of these features reveals that the majority of them represent loops, terminal regions, and helices, indicating that these secondary-structure elements mediate the formation of glycosyltransferases' homooligomers and directly contribute to the specific binding. We also observe relatively short protein regions that disrupt the homodimer interactions, although such cases are rare. These results suggest that relatively small structural changes in the nonconserved regions may contribute to the formation of different functional oligomeric states and might be important in regulation of enzyme activity through homooligomerization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.