ArticlePlant physiology2001
Characterization of a functional soluble form of a Brassica napus membrane-anchored endo-1,4-beta-glucanase heterologously expressed in Pichia pastoris.
Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 90 citations in OpenAlex.
- Barley roots require HvGLU3 for cellulose biosynthesis.Plant physiology · 2025Article
- The putative endo-1,4-β-D-glucanase GLU3 regulates cellulose biosynthesis in barley roots.Plant physiology · 2025Article
- Recent Developments in Deciphering the Biological Role of Plant ComplexFrontiers in plant science · 2022Review
- Arabidopsis thaliana KORRIGAN1 protein: N-glycan modification, localization, and function in cellulose biosynthesis and osmotic stress responses.Plant signaling & behavior · 2015Article
- The trafficking of the cellulose synthase complex in higher plants.Annals of botany · 2014Review
- Cellulase in Cellulose Synthase: A Cat among the Pigeons?Plant physiology · 2014Article
- The Cellulase KORRIGAN Is Part of the Cellulose Synthase Complex.Plant physiology · 2014Article
- Cellulose synthesis and its regulation.The arabidopsis book · 2014Article
- KORRIGAN1 interacts specifically with integral components of the cellulose synthase machinery.PloS one · 2014Article
- Systematic screening of glycosylation- and trafficking-associated gene knockouts in Saccharomyces cerevisiae identifies mutants with improved heterologous exocellulase activity and host secretion.BMC biotechnology · 2013Article
- Characterizing the link between glycosylation state and enzymatic activity of the endo-β1,4-glucanase KORRIGAN1 from Arabidopsis thaliana.The Journal of biological chemistry · 2013Article
- Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses.Plant physiology · 2013Article
- Global identification of multiple OsGH9 family members and their involvement in cellulose crystallinity modification in rice.PloS one · 2013Article
- Endo-(1,4)-β-glucanase gene families in the grasses: temporal and spatial co-transcription of orthologous genes.BMC plant biology · 2012Article
- Secretion and activity of antimicrobial peptide cecropin D expressed in Pichia pastoris.Experimental and therapeutic medicine · 2012Article
- Developmental consequences of the tumorous shoot development1 mutation, a novel allele of the cellulose-synthesizing KORRIGAN1 gene.Plant molecular biology · 2009Article
- Assay and heterologous expression in Pichia pastoris of plant cell wall type-II membrane anchored glycosyltransferases.Glycoconjugate journal · 2009Article
- Expression of SARS-coronavirus spike glycoprotein in Pichia pastoris.Virus genes · 2009Article
- Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Brassica napus gene, Cel16, encodes a membrane-anchored endo-1,4-beta-glucanase with a deduced molecular mass of 69 kD. As for other membrane-anchored endo-1,4-beta-glucanases, Cel16 consists of a predicted intracellular, charged N terminus (methionine(1)-lysine(70)), a hydrophobic transmembrane domain (isoleucine(71)-valine(93)), and a periplasmic catalytic core (lysine(94)-proline(621)). Here, we report the functional analysis of Delta(1-90)Cel16, the N terminally truncated Cel16, missing residues 1 through 90 and comprising the catalytic domain of Cel16 expressed recombinantly in the methylotrophic yeast Pichia pastoris as a soluble protein. A two-step purification protocol yielded Delta(1-90)Cel16 in a pure form. The molecular mass of Delta(1-90)Cel16, when determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was about 130 kD and about 60 kD after enzymatic removal of N-glycans, fitting the expected molecular mass of 59 kD. Delta(1-90)Cel16 was highly N glycosylated as compared with the native B. napus Cel16 protein. Delta(1-90)Cel16 had a pH optimum of 6.0. The activity of Delta(1-90)Cel16 was inhibited by EDTA and exhibited a strong dependence on calcium. Delta(1-90)Cel16 showed substrate specificity for low substituted carboxymethyl-cellulose and amorphous cellulose. It did not hydrolyze crystalline cellulose, xyloglycan, xylan, (1-->3),(1-->4)-beta-D-glucan, the highly substituted hydroxyethylcellulose, or the oligosaccharides cellotriose, cellotetraose, cellopentaose, or xylopentaose. Size exclusion analysis of Delta(1-90)Cel16-hydrolyzed carboxymethylcellulose showed that Delta(1-90)Cel16 is a true endo-acting glucanase.
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