ArticlePlant physiology2001
The catalytic site of the pectin biosynthetic enzyme alpha-1,4-galacturonosyltransferase is located in the lumen of the Golgi.
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 61 papers.
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Who cites it
61 citing papers in PubMed, 142 citations in OpenAlex.
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- Homogalacturonan Pectins Tuned as an Effect of Susceptible rbohD, Col-0-Reactions, and Resistance rbohF-, rbohD/F-Reactions to TuMV.International journal of molecular sciences · 2024Article
- Design of a Protein with Improved Thermal Stability by an Evolution-Based Generative Model.Angewandte Chemie (International ed. in English) · 2022Article
- Multi-Omics Approaches to Improve Clubroot Resistance in Brassica with a Special Focus onInternational journal of molecular sciences · 2022Review
- Identification and expression analysis of the3 Biotech · 2022Article
- Cell biology of primary cell wall synthesis in plants.The Plant cell · 2022Review
- Two galacturonosyltransferases function in plant growth, stomatal development, and dynamics.Plant physiology · 2021Article
- Amplification, sequencing and characterization of pectin methyl esterase inhibitor 51 gene inSaudi journal of biological sciences · 2021Article
- Cell wall associated immunity in plants.Stress biology · 2021Review
- A Golgi-localized manganese transporter functions in pollen tube tip growth to control male fertility inPlant communications · 2021Article
- Article
- Insights into the molecular control of cross-incompatibility in Zea mays.Plant reproduction · 2020Review
- Genome-wide association analysis of sucrose concentration in soybean (Glycine max L.) seed based on high-throughput sequencing.The plant genome · 2020Article
- Pectin Synthesis and Pollen Tube Growth inFrontiers in plant science · 2020Article
- New steps in mucilage biosynthesis revealed by analysis of the transcriptome of the UDP-rhamnose/UDP-galactose transporter 2 mutant.Journal of experimental botany · 2019Article
- The Dynamic Responses of Cell Walls in Resurrection Plants During Dehydration and Rehydration.Frontiers in plant science · 2019Review
- Critical Review of Plant Cell Wall Matrix Polysaccharide Glycosyltransferase Activities Verified by Heterologous Protein Expression.Frontiers in plant science · 2019Review
- Genome-Wide Identification and Characterization of Pectin Methylesterase Inhibitor Genes inInternational journal of molecular sciences · 2018Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-1,4-galacturonosyltransferase (GalAT) is an enzyme required for the biosynthesis of the plant cell wall pectic polysaccharide homogalacturonan (HGA). GalAT activity in homogenates from pea (Pisum sativum L. var. Alaska) stem internodes co-localized in linear and discontinuous sucrose gradients with latent UDPase activity, an enzyme marker specific for Golgi membranes. GalAT activity was separated from antimycin A-insensitive NADH:cytochrome c reductase and cytochrome c oxidase activities, enzyme markers for the endoplasmic reticulum and the mitochondria, respectively. GalAT and latent UDPase activities were separated from the majority (80%) of callose synthase activity, a marker for the plasma membrane, suggesting that little or no GalAT is present in the plasma membrane. GalAT activities in proteinase K-treated and untreated Golgi vesicles were similar, whereas no GalAT activity was detected after treating Golgi vesicles with proteinase K in the presence of Triton X-100. These results demonstrate that the catalytic site of GalAT resides within the lumen of the Golgi. The products generated by Golgi-localized GalAT were converted by endopolygalacturonase treatment to mono- and di-galacturonic acid, thereby showing that GalAT synthesizes 1-->4-linked alpha-D-galacturonan. Our data provide the first enzymatic evidence that a glycosyltransferase involved in HGA synthesis is present in the Golgi apparatus. Together with prior results of in vivo labeling and immunocytochemical studies, these results show that pectin biosynthesis occurs in the Golgi. A model for the biosynthesis of the pectic polysaccharide HGA is proposed.
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