A characterization of recombinant Arabidopsis FRIABLE1 (FRB1) reveals robust rhamnogalacturonan-I rhamnosyltransferase activity and critical catalytic residues.

Kayleigh J Robichaux, Madison N Blea, Robert A Amos, Chin Huang, Debra Mohnen, Ian S Wallace

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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6 authors.

Kayleigh J RobichauxDepartment of Biochemistry and Molecular Biology, University of Nevada, Reno, Reno, Nevada, USA.

Madison N BleaDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA.

Robert A AmosDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA.

Chin HuangDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA.

Debra MohnenDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA.

Ian S WallaceDepartment of Biochemistry and Molecular Biology, University of Nevada, Reno, Reno, Nevada, USA; Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA. Electronic address: ian.wallace@uga.edu.

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6 · The paper itself

Abstract

Plant cell walls are glycan-rich extracellular matrices that fundamentally impact essential cellular processes, such as growth, adhesion, and cell shape acquisition. Understanding plant cell wall glycans requires the identification and characterization of the biosynthetic enzymes that produce these polymers. Most successful in vitro protein expression studies of plant cell wall glycosyltransferases have relied on insect, fungal/yeast, or human cell expression systems, whereas prokaryotic expression systems have been generally unsuccessful. Here, we show that Arabidopsis FRIABLE1 (FRB1)/rhamnogalacturonan-I rhamnosyltransferase 8 (RRT8) can be produced in Escherichia coli RosettaGami2 cells as N-terminal maltose-binding protein fusion proteins containing C-terminal 6X-His-tags. We also report the catalytic constants of FRB1/RRT8 with apparent K

Indexed as

ArabidopsisArabidopsis ProteinsHexosyltransferasesPectinsBiocatalysisEscherichia coliRecombinant ProteinsArabidopsis ProteinsHexosyltransferasesPectinsRecombinant Proteinsrhamnogalacturonan Iglycosyltransferasepectin biosynthesisplant cell wallrhamnogalacturonan-I

Identifiers

PMID41724380

DOI10.1016/j.jbc.2026.111305

PMCPMC13010939

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