title: Differential expression of α-L-arabinofuranosidases during maize (Zea mays L.) root elongation.
abstract: Specific α- l -arabinofuranosidases are involved in the realisation of elongation growth process in cells with type II cell walls. Elongation growth in a plant cell is largely based on modification of the cell wall. In type II cell walls, the Ara/Xyl ratio is known to decrease during elongation due to the partial removal of Ara residues from glucuronoarabinoxylan. We searched within the maize genome for the genes of all predicted α-L-arabinofuranosidases that may be responsible for such a process and related their expression to the activity of the enzyme and the amount of free arabinose measured in six zones of a growing maize root. Eight genes of the GH51 family (ZmaABFs) and one gene of the GH3 family (ZmaARA-I) were identified. The abundance of ZmaABF1 and 3-6 transcripts was highly correlated with the measured enzymatic activity and free arabinose content that significantly increased during elongation. The transcript abundances also coincided with the pattern of changes in the Ara/Xyl ratio of the xylanase-extractable glucuronoarabinoxylan described in previous studies. The expression of ZmaABF3, 5 and 6 was especially up-regulated during elongation although corresponding proteins are devoid of the catalytic glutamate at the proper position. ZmaABF2 transcripts were specifically enriched in the root cap and meristem. A single ZmaARA-I gene was not expressed as a whole gene but instead as splice variants that encode the C-terminal end of the protein. Changes in the ZmaARA-I transcript level were rather moderate and had no significant correlation with free arabinose content. Thus, elongation growth of cells with type II cell walls is accompanied by the up-regulation of specific and predicted α-L-arabinofuranosidase genes, and the corresponding activity is indeed pronounced and is important for the modification of glucuronoarabinoxylan, which plays a key role in the modification of the cell wall supramolecular organisation.
authors.affiliation: Kazan Scientific Center, Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, Lobachevsky 2/31, p.o. 30, 420111, Kazan, Russia, bbinb@bk.ru.
authors.forename: Liudmila V
authors.initials: LV
authors.lastname: Kozlova
authors.forename: Oleg V
authors.initials: OV
authors.lastname: Gorshkov
authors.forename: Natalia E
authors.initials: NE
authors.lastname: Mokshina
authors.forename: Tatyana A
authors.initials: TA
authors.lastname: Gorshkova
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017343:Genes, Plant; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D018517:Plant Roots / Q000254:growth & development*; D017386:Sequence Homology, Amino Acid; D003313:Zea mays / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development
chemical_list: D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase