ArticlePlant molecular biology2001
DcAGP1, a secreted arabinogalactan protein, is related to a family of basic proline-rich proteins.
Article in Plant molecular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 57 citations in OpenAlex.
- Allelic Expression Dynamics of Regulatory Factors During Embryogenic Callus Induction in ABB Banana (Plants (Basel, Switzerland) · 2025Article
- Arabinogalactan-Proteins as Boron-Acting Enzymes, Cross-Linking the Rhamnogalacturonan-II Domains of Pectin.Plants (Basel, Switzerland) · 2023Review
- Making and breaking of boron bridges in the pectic domain rhamnogalacturonan-II at apoplastic pH in vivo and in vitro.The Plant journal : for cell and molecular biology · 2023Article
- An Arabidopsis thaliana arabinogalactan-protein (AGP31) and several cationic AGP fragments catalyse the boron bridging of rhamnogalacturonan-II.The Biochemical journal · 2022Article
- The Arabinogalactan Protein Family ofPlants (Basel, Switzerland) · 2021Article
- The Cell Wall PAC (Proline-Rich, Arabinogalactan Proteins, Conserved Cysteines) Domain-Proteins Are Conserved in the Green Lineage.International journal of molecular sciences · 2020Article
- Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development inFrontiers in plant science · 2020Article
- HyPRP1 performs a role in negatively regulating cotton resistance to V. dahliae via the thickening of cell walls and ROS accumulation.BMC plant biology · 2018Article
- Bioinformatics Prediction and Evolution Analysis of Arabinogalactan Proteins in the Plant Kingdom.Frontiers in plant science · 2017Article
- Differential proteome analysis during early somatic embryogenesis in Musa spp. AAA cv. Grand Naine.Plant cell reports · 2017Article
- Post-Translational Modification and Secretion of Azelaic Acid Induced 1 (AZI1), a Hybrid Proline-Rich Protein from Arabidopsis.International journal of molecular sciences · 2016Article
- Arabinogalactan protein 31 (AGP31), a putative network-forming protein in Arabidopsis thaliana cell walls?Annals of botany · 2014Article
- An update on post-translational modifications of hydroxyproline-rich glycoproteins: toward a model highlighting their contribution to plant cell wall architecture.Frontiers in plant science · 2014Review
- Arabinogalactan proteins in root and pollen-tube cells: distribution and functional aspects.Annals of botany · 2012Review
- Characterization of the arabinogalactan protein 31 (AGP31) of Arabidopsis thaliana: new advances on the Hyp-O-glycosylation of the Pro-rich domain.The Journal of biological chemistry · 2012Article
- A bioinformatics approach to the identification, classification, and analysis of hydroxyproline-rich glycoproteins.Plant physiology · 2010Article
- Proteomic analysis of somatic embryogenesis in Valencia sweet orange (Citrus sinensis Osbeck).Plant cell reports · 2009Article
- Genome-wide transcriptional analysis of super-embryogenic Medicago truncatula explant cultures.BMC plant biology · 2008Article
- A nonclassical arabinogalactan protein gene highly expressed in vascular tissues, AGP31, is transcriptionally repressed by methyl jasmonic acid in Arabidopsis.Plant physiology · 2007Article
- Characterization of expressed sequence tags obtained by SSH during somatic embryogenesis in Cichorium intybus L.BMC plant biology · 2007Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A cDNA corresponding to the core protein of an immunoaffinity-purified arabinogalactan protein (AGP) secreted aucus carota (carrot) cells in liquid culture was isolated. This cDNA, DcAGP1, encodes a new class of non-classical' AGP with strong similarity to a family of basic proline-rich proteins. The protein is rich in proline (17%), alanine (10%) and lysine (11%) and contains four distinct domains: a signal peptide, a proline-rich domain, a histidine-rich basic domain and a cysteine-containing 'PAC' domain that is found in a range of other cell wall proteins. The protein contains several sequence motifs found in otherwise unrelated cell wall proteins, but also displays some unique features. Northern blot analyses show that while the DcAGP1 transcript is abundant in the suspension-culture cells from which the AGP was obtained; in carrot seedlings the gene is only expressed at low levels in the roots and it is neither wound- nor stress-inducible. Furthermore, northern and western blot analyses demonstrate that the core polypeptide of DcAGP1 is differentially glycosylated in two different carrot suspension cultures. The unusual features of the protein sequence suggest that the DcAGP1 protein is a member of a family of basic proline-rich proteins defined by the C-terminal PAC domain, and the possible function(s) of the DcAGP1 protein is considered in the light of current views on AGP structure and function.
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