ArticlePlanta2004
Subcellular localization and topology of beta(1-->4)galactosyltransferase that elongates beta(1-->4)galactan side chains in rhamnogalacturonan I in potato.
Article in Planta, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Amplification, sequencing and characterization of pectin methyl esterase inhibitor 51 gene inSaudi journal of biological sciences · 2021Article
- Pectin and Pectin-Based Composite Materials: Beyond Food Texture.Molecules (Basel, Switzerland) · 2018Review
- Pectin biosynthesis: GALS1 in Arabidopsis thaliana is a β-1,4-galactan β-1,4-galactosyltransferase.The Plant cell · 2012Article
- Biosynthesis of pectin.Plant physiology · 2010Review
- Regulation of adipocyte differentiation by distinct subcellular pools of protein kinase B (PKB/Akt).The Journal of biological chemistry · 2010Article
- Exploring the ultrastructural localization and biosynthesis of beta(1,4)-galactan in Pinus radiata compression wood.Plant physiology · 2009Article
- Article
- Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II.The Plant cell · 2006Article
- A complementary bioinformatics approach to identify potential plant cell wall glycosyltransferase-encoding genes.Plant physiology · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The subcellular localization and topology of rhamnogalacturonan I (RG-I) beta(1-->4)galactosyltransferase(s) (beta[1-->4]GalTs) from potato ( Solanum tuberosum L.) were investigated. Using two-step discontinuous sucrose step gradients, galactosyltransferase (GalT) activity that synthesized 70%-methanol-insoluble products from UDP-[(14)C]Gal was detected in both the 0.5 M sucrose fraction and the 0.25/1.1 M sucrose interface. The former fraction contained mainly soluble proteins and the latter was enriched in Golgi vesicles that contained most of the UDPase activity, a Golgi marker. By gel-filtration analysis, products of 180-2000 Da were found in the soluble fraction, whereas in the Golgi-enriched fraction the products were larger than 80 kDa and could be digested with rhamnogalacturonan lyase and beta(1,4) endogalactanase to yield smaller rhamnogalacturonan oligomers, galactobiose and galactose. The endogalactanase requires beta(1-->4)galactans with at least three galactosyl residues for cleavage, indicating that the enzyme(s) present in the 0.25/1.1 M Suc interface transferred one or more galactosyl residues to pre-existing beta(1-->4)galactans producing RG-I side chains in total longer than a trimer. Thus, the beta(1-->4)GalT activity that elongates beta(1-->4)-linked galactan on RG-I was located in the Golgi apparatus. This beta(1-->4)GalT activity was not reduced after treatment of the Golgi vesicles with proteinase, but approximately 75% of the activity was lost after treatment with proteinase in the presence of Triton X-100. In addition, the beta(1-->4)GalT activity was recovered in the detergent phase after treatment of Golgi vesicles with Triton X-114. Taken together, these observations supported the view that the RG-I beta(1-->4)GalT that elongates beta(1-->4)galactan was mainly located in the Golgi apparatus and integrated into the membrane with its catalytic site facing the lumen.
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