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Diversity of Pectin Rhamnogalacturonan I Rhamnosyltransferases in Glycosyltransferase Family 106.

Authors :
Wachananawat, Bussarin
Kuroha, Takeshi
Takenaka, Yuto
Kajiura, Hiroyuki
Naramoto, Satoshi
Yokoyama, Ryusuke
Ishizaki, Kimitsune
Nishitani, Kazuhiko
Ishimizu, Takeshi
Source :
Frontiers in Plant Science; 7/2/2020, Vol. 11, p1-12, 12p
Publication Year :
2020

Abstract

Rhamnogalacturonan I (RG-I) comprises approximately one quarter of the pectin molecules in land plants, and the backbone of RG-I consists of a repeating sequence of [2)-α-L-Rha(1-4)-α-D-GalUA(1-] disaccharide. Four Arabidopsis thaliana genes encoding RG-I rhamnosyltransferases (AtRRT1 to AtRRT4), which synthesize the disaccharide repeats, have been identified in the glycosyltransferase family (GT106). However, the functional role of RG-I in plant cell walls and the evolutional history of RRTs remains to be clarified. Here, we characterized the sole ortholog of AtRRT1–AtRRT4 in liverwort, Marchantia polymorpha , namely, MpRRT1. MpRRT1 had RRT activity and genetically complemented the At RRT1 -deficient mutant phenotype in A. thaliana. However, the Mp RRT1 -deficient M. polymorpha mutants showed no prominent morphological changes and only an approximate 20% reduction in rhamnose content in the cell wall fraction compared to that in wild-type plants, suggesting the existence of other RRT gene(s) in the M. polymorpha genome. As expected, we detected RRT activities in other GT106 family proteins such as those encoded by Mp RRT3 in M. polymorpha and FRB1/ At RRT8 in A. thaliana , the deficient mutant of which affects cell adhesion. Our results show that RRT genes are more redundant and diverse in GT106 than previously thought. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
1664462X
Volume :
11
Database :
Complementary Index
Journal :
Frontiers in Plant Science
Publication Type :
Academic Journal
Accession number :
144374377
Full Text :
https://doi.org/10.3389/fpls.2020.00997