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dc.contributor.author
Strasser, Richard
dc.contributor.author
Seifert, Georg
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Doblin, Monika S.
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Johnson, Kim L.
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Ruprecht, Colin
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Pfrengle, Fabian
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dc.contributor.author
Bacic, Antony
dc.contributor.author
Estevez, Jose Manuel
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dc.date.available
2021-09-28T12:12:41Z
dc.date.issued
2021-02
dc.identifier.citation
Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-19
dc.identifier.issn
1664-462X
dc.identifier.uri
http://hdl.handle.net/11336/141685
dc.description.abstract
Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Frontiers Media
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
ARABIDOPSIS
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GLYCAN ARRAYS
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GLYCAN FUNCTIONS
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GLYCOSYL HYDROLASES
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GLYCOSYLTRANSFERASES
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N-GLYCOSYLATION
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O-GLYCOSYLATION
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PLANT PROTEIN GLYCOSYLATION
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
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dc.title
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-09-15T15:20:06Z
dc.journal.volume
12
dc.journal.pagination
1-19
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Lausanne
dc.description.fil
Fil: Strasser, Richard. University of Natural Resources and Life Sciences; Suiza
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Fil: Seifert, Georg. University of Natural Resources and Life Sciences; Suiza
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Fil: Doblin, Monika S.. La Trobe University; Australia
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Fil: Johnson, Kim L.. La Trobe University; Australia
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Fil: Ruprecht, Colin. University of Natural Resources and Life Sciences; Suiza
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Fil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; Suiza
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Fil: Bacic, Antony. La Trobe University; Australia
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Fil: Estevez, Jose Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.journal.title
Frontiers in Plant Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.640919/full
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fpls.2021.640919
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