ArticleThe Journal of biological chemistry2011
Structure-function analysis of the bacterial expansin EXLX1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- O-Glycosylated expansinScience advances · 2026Article
- Catalysis does not explain expansin-mediated wall creep: Distinguishing catalytic ERPs from creep-active expansins.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Reply to Cosgrove: Catalytic activity in expansin-like proteins does not explain wall creep but raises a flag.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Zwitterion Moieties in Polypeptides Synergistically Enhance the Release of Cellulose and Amorphous Polysaccharides from Plant Cell Walls.Biomacromolecules · 2026Article
- Functional characterization of a dockerin-containing expansin-like protein from the anaerobic fungus Neocallimastix californiae.Biotechnology for biofuels and bioproducts · 2026Article
- Uncovering Sequence and Structural Characteristics of Fungal Expansin-Related Proteins With Potential to Drive Substrate Targeting.Proteins · 2026Article
- A single-domain expansin-like protein fromProceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Lotus japonicus alpha-expansin EXPA1 is recruited during intracellular and intercellular rhizobial colonization.The Plant journal : for cell and molecular biology · 2025Article
- Wild rice-associatedmSystems · 2025Article
- The Bacillus subtilis expansin BsEXLX1 enhances cellobiohydrolase I activity on sugar beet pulp as shown by QCM-D.Biotechnology letters · 2025Article
- Carbohydrate-binding domain CBM63 of microbial expansin-like BsEXLX1 facilitates the adsorption of expansin-related proteins to hemicelluloses in plant secondary cell walls.Biotechnology for biofuels and bioproducts · 2025Article
- SANS investigation of fungal loosenins reveals substrate-dependent impacts of protein action on the inter-microfibril arrangement of cellulosic substrates.Biotechnology for biofuels and bioproducts · 2025Article
- Aromatic residues in N-terminal domain of archaeal trehalase affect the folding and activity of catalytic domain.Applied microbiology and biotechnology · 2024Article
- Alpha-expansins: more than three decades of wall creep and loosening in fruits.Plant molecular biology · 2024Review
- Role of Natural Binding Proteins in Therapy and Diagnostics.Life (Basel, Switzerland) · 2024Article
- Structure and growth of plant cell walls.Nature reviews. Molecular cell biology · 2024Review
- Insights into the action of phylogenetically diverse microbial expansins on the structure of cellulose microfibrils.Biotechnology for biofuels and bioproducts · 2024Article
- Hormone-regulated expansins: Expression, localization, and cell wall biomechanics in Arabidopsis root growth.Plant physiology · 2023Article
- Bacterial surface-exposed lipoproteins and sortase-mediated anchored cell surface proteins in plant infection.MicrobiologyOpen · 2023Review
- Loosenin-Like Proteins fromApplied and environmental microbiology · 2023Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We made use of EXLX1, an expansin from Bacillus subtilis, to investigate protein features essential for its plant cell wall binding and wall loosening activities. We found that the two expansin domains, D1 and D2, need to be linked for wall extension activity and that D2 mediates EXLX1 binding to whole cell walls and to cellulose via distinct residues on the D2 surface. Binding to cellulose is mediated by three aromatic residues arranged linearly on the putative binding surface that spans D1 and D2. Mutation of these three residues to alanine eliminated cellulose binding and concomitantly eliminated wall loosening activity measured either by cell wall extension or by weakening of filter paper but hardly affected binding to whole cell walls, which is mediated by basic residues located on other D2 surfaces. Mutation of these basic residues to glutamine reduced cell wall binding but not wall loosening activities. We propose domain D2 as the founding member of a new carbohydrate binding module family, CBM63, but its function in expansin activity apparently goes beyond simply anchoring D1 to the wall. Several polar residues on the putative binding surface of domain D1 are also important for activity, most notably Asp82, whose mutation to alanine or asparagine completely eliminated wall loosening activity. The functional insights based on this bacterial expansin may be extrapolated to the interactions of plant expansins with cell walls.
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