Expression of the C-terminal family 22 carbohydrate-binding module of xylanase 10B of Clostridium themocellum in tobacco plant

Abstract

Carbohydrate-binding modules have been shown to alter plant cell wall structural architecture. Hence, they have the potential application of being used to engineer the plant to produce tailor-made natural fibers in the cell wall. The Clostridium thermocellum xylanase, Xyn10B, contains two CBMs that belong to family 22 (CBM22). The C-terminal CBM22-2 of the glycoside hydrolase (GH) 10 had been characterized to interact with xylan, a major hemicellulosic component in the secondary cell wall of plants. In this work, the expression of the CBM22-2 in transgenic tobacco plants was evaluated. Histological examinations of the transgenic stems did not reveal marked cell wall phenotype. In addition, there were no observable changes in the height or the appearance of the transgenic plants expressing the CBM22-2 module. The results indicate that the family 22 carbohydrate binding module is not a potential candidate for use in in planta modification of the cell wall.

A diverse set of Enterococcus-infecting phage provides insight into phage host-range determinants

“…The models of the N-terminal and c-terminal portions structurally align both with each other and with the CBM domains of a xylanase from Paenibacillus barcinonensis (PDB model 4XUP) that is predicted to encode a sugar-binding domain of the CBM22 tandem domain family (CAZy , ( Drula et al, 2022 )). These and related CBM domains have been shown in various organisms to bind carbohydrate polymers ( Devillard et al, 2003 ; Obembe, 2009 ; Sainz-Polo et al, 2015 ). In the context of phage and enterococci, this may suggest targeting of carbohydrate structures on bacterial surfaces such as those within EPA ( Guerardel et al, 2020 ).…”