Gibberellin Oxidase Gene Family in L. chinense: Genome-Wide Identification and Gene Expression Analysis.

GAox is a key enzyme for the transformation of gibberellins, and belongs to the 2-ketoglutarate dependent dioxygenase gene family (2ODD). However, a systematic analysis of GAox in the angiosperm L. chinense has not yet been reported. Here, we identified all LcGAox gene family members in L. chinense, which were classified into the three subgroups of GA20ox, C19GA2ox, and C20GA2ox. Comparison of the gene structure, conserve motifs, phylogenetic relationships, and syntenic relationships of gibberellin oxidase gene families in different species indicated that the gene functional differences may be due to the partial deletion of their domains during evolution. Furthermore, evidence for purifying selection was detected between orthologous GAox genes in rice, grape, Arabidopsis, and L. chinense. Analysis of the codon usage patterns showed that mutation pressure and natural selection might have induced codon usage bias in angiosperms; however, the LcGAox genes in mosses, lycophytes, and ambarella plants exhibited no obvious codon usage preference. These results suggested that the gibberellin oxidase genes were more primitive. The gene expression pattern was analyzed in different organs subjected to multiple abiotic stresses, including GA, abscisic acid (ABA), and chlormequat (CCC) treatment, by RNA-seq and qRT-PCR, and the stress- and phytohormone-responsive cis-elements were counted. The results showed that the synthesis and decomposition of GA were regulated by different LcGAox genes in the vegetative and reproductive organs of L. chinense, and only LcGA2ox1,4, and 7 responded to the NaCl, polyethylene glycol, 4 °C, GA, ABA, and CCC treatment in the roots, stems, and leaves of seedlings at different time periods, revealing the potential role of LcGAox in stress resistance.

Structural characterization of the lignin-carbohydrate complex in biomass pretreated with Fenton oxidation and hydrothermal treatment and consequences on enzymatic hydrolysis efficiency.

In this study, lignin-carbohydrate complexes (LCCs) were isolated from biomass (raw and pretreated) to investigate the structural changes in biomass pretreated by Fenton oxidation and hydrothermal treatment, and their effect on enzymatic hydrolysis. The composition and structure of the LCCs fractions were investigated via carbohydrate analysis, XRD, FT-IR, and 2D HSQC NMR. The biomass degradation rate of yellow poplar and larch during Fenton oxidation and hydrothermal treatment was approximately 30%. Most of the hemicellulose was degraded during pretreatment, while xylan remained in the yellow poplar, and galactan, mannan, and xylan remained in the larch. The fractional yield of glucan-rich LCC (LCC1) in the yellow poplar (raw and pretreated biomass) was high, while that of glucomannan-rich LCC (LCC3) in larch was higher than the yield yellow poplar. Phenyl glycoside, γ-ester, and benzyl ether linkages were observed in the LCCs of yellow poplar, while phenyl glycoside and γ-ester were detected in those of larch. Following pretreatment, the frequencies of ß-ß', ß-5, and γ-ester in the LCCs of larch were found to be higher than in those of yellow poplar. The efficiencies of enzymatic hydrolysis for the pretreated yellow poplar and larch were 93.53% and 26.23%, respectively. These finding indicated that the ß-ß', ß-5, and γ-ester linkages included in the pretreated biomass affected the efficiency of enzymatic hydrolysis.

Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera.

Ferroxidase activity was detected in a laccase-like multicopper oxidase (LMCO) produced in transgenic tobacco cells expressing an LMCO cDNA (Ltlacc2.2) cloned from yellow-poplar (Liriodendron tulipifera). This marks the first report of ferroxidase activity associated with a plant laccase and suggests that some members of this plant enzyme family may have physiological functions based on activities other than their more widely recognized phenoloxidase activity. Recent work with LMCOs from bacteria, yeast and mammals has shown that metal oxidase activities in these enzymes can be important for their primary physiological functions, With respect to ferroxidase activity in certain plant LMCOs, it is proposed that the high levels of LMCO expression in plant vascular tissues may reflect the need for high-efficiency iron uptake pumps in tissues that undergo lignification during normal development. Such iron uptake pumps would function to minimize levels of free iron so that reactive oxygen species do not reach toxic levels when H2O2 is generated for peroxidase-mediated monolignol coupling during lignin deposition.