NDLI: Group III-A XTH Genes of Arabidopsis Encode Predominant Xyloglucan Endohydrolases That Are Dispensable for Normal Growth 1 [C] [W] [OA]

Content Provider	PubMed Central
Author	Kaewthai, Nomchit Gendre, Delphine Eklöf, Jens M. Ibatullin, Farid M. Ezcurra, Ines Bhalerao, Rishikesh P. Brumer, Harry
Copyright Year	2013
Abstract	The molecular basis of primary wall extension endures as one of the central enigmas in plant cell morphogenesis. Classical cell wall models suggest that xyloglucan endo-transglycosylase activity is the primary catalyst (together with expansins) of controlled cell wall loosening through the transient cleavage and religation of xyloglucan-cellulose cross links. The genome of Arabidopsis (Arabidopsis thaliana) contains 33 phylogenetically diverse XYLOGLUCAN ENDO-TRANSGLYCOSYLASE/HYDROLASE (XTH) gene products, two of which were predicted to be predominant xyloglucan endohydrolases due to clustering into group III-A. Enzyme kinetic analysis of recombinant AtXTH31 confirmed this prediction and indicated that this enzyme had similar catalytic properties to the nasturtium (Tropaeolum majus) xyloglucanase1 responsible for storage xyloglucan hydrolysis during germination. Global analysis of Genevestigator data indicated that AtXTH31 and the paralogous AtXTH32 were abundantly expressed in expanding tissues. Microscopy analysis, utilizing the resorufin β-glycoside of the xyloglucan oligosaccharide XXXG as an in situ probe, indicated significant xyloglucan endohydrolase activity in specific regions of both roots and hypocotyls, in good correlation with transcriptomic data. Moreover, this hydrolytic activity was essentially completely eliminated in AtXTH31/AtXTH32 double knockout lines. However, single and double knockout lines, as well as individual overexpressing lines, of AtXTH31 and AtXTH32 did not demonstrate significant growth or developmental phenotypes. These results suggest that although xyloglucan polysaccharide hydrolysis occurs in parallel with primary wall expansion, morphological effects are subtle or may be compensated by other mechanisms. We hypothesize that there is likely to be an interplay between these xyloglucan endohydrolases and recently discovered apoplastic exo-glycosidases in the hydrolytic modification of matrix xyloglucans.
Related Links	http://dx.doi.org/10.1104/pp.112.207308
Ending Page	454
Page Count	15
Starting Page	440
File Format	PDF
ISSN	15322548
e-ISSN	15322548
Journal	Plant Physiology
Issue Number	1
Volume Number	161
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2013-01-01
Access Restriction	Open
Rights Holder	American Society of Plant Biologists
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Physiology Plant Science

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