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MALE GAMETOPHYTE DEFECTIVE 4 encodes a rhamnogalacturonan II xylosyltransferase and is important for growth of pollen tubes and roots in Arabidopsis
Author(s) -
Liu XiaoLei,
Liu Lifeng,
Niu QianKun,
Xia Chuan,
Yang KeZhen,
Li Rui,
Chen LiQun,
Zhang XueQin,
Zhou Yihua,
Ye De
Publication year - 2011
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2010.04452.x
Subject(s) - pollen tube , arabidopsis , mutant , pollen , gametophyte , biology , xylose , microbiology and biotechnology , pichia pastoris , cell wall , biochemistry , botany , gene , pollination , fermentation , recombinant dna
Summary In flowering plants, the growth of pollen tubes is essential for the delivery of sperm to the egg cells. Although many factors (including cell‐wall properties) are involved in this process, little is known about the underlying molecular mechanisms that regulate the growth of pollen tubes. We report here the characterization of an Arabidopsis mutant male gametophyte defective 4 ( mgp4 ) that is severely defective in pollen tube growth. The mgp4 mutation also impairs root growth of pollen‐rescued mgp4 mutant plants generated by expressing MGP4 cDNA under the control of a pollen grain/tube‐specific promoter. The MGP4 gene encodes a putative xylosyltransferase and is expressed in many organs/tissues, including pollen tubes and roots. MGP4 protein expressed in Pichia pastoris exhibited xylosyltransferase activity and transferred d ‐xylose onto l ‐fucose. The pectic polysaccharide rhamnogalacturonan II (RG‐II), isolated from 7‐day‐old pollen‐rescued mutant seedlings, exhibited a 30% reduction in 2‐ O‐ methyl d ‐xylose residues. Furthermore, an exogenous supply of boric acid enhanced RG‐II dimer formation and partially restored the root growth of the pollen‐rescued mutant seedlings. Taken together, these results suggest that MGP4 plays important roles in pollen tube and root growth by acting as a xylosyltransferase involved in the biosynthesis of pectic RG‐II.