Comprehensive Analysis of Rice Laccase Gene (OsLAC) Family and Ectopic Expression of OsLAC10 Enhances Tolerance to Copper Stress in Arabidopsis

Liu, Qingquan; Luo, Le; Wang, Xiaoxiao; Shen, Zhenguo; Zheng, Luqing

doi:10.3390/ijms18020209

Cited by 115 publications

(96 citation statements)

References 55 publications

(86 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, OsmiR397, OsmiR398 and OsmiR408 also play an important role in abiotic and biotic stress responses (Jia et al ., ; Lu et al ., ; Pan et al ., ). OsLAC8 and OsLAC29 were significantly induced by salt stress in both salt‐sensitive cultivars (Liu et al ., ). Therefore, we hypothesized that OsAGO17 may respond to stress in rice.…”

Section: Discussionmentioning

confidence: 99%

“…In our study, three LAC genes showed the same change in expression as OsLAC, and the expression patterns of these genes were complementary to that of OsAGO17. OsLAC14 is a homologue of OsLAC (Liu et al, 2017). Thus, OsLAC may not be the only target gene of OsmiR397b in the regulation of grain size, and OsAGO17 may affect grain size by regulating the expression of other LAC genes.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

A putative AGO protein, OsAGO17, positively regulates grain size and grain weight through OsmiR397b in rice

Zhong

Zhu

et al. 2019

Plant Biotechnology Journal

View full text Add to dashboard Cite

Summary Argonaute (AGO) proteins and small RNAs (sRNAs) are core components of the RNA‐induced silencing complex (RISC). It has been reported that miRNAs regulate plant height and grain size in rice, but which AGO is involved in grain size regulation remains unclear. Here, we report that enhanced expression of OsAGO17, a putative AGO protein, could improve grain size and weight and promote stem development in rice. Cytological evidence showed that these effects are mainly caused by alteration of cell elongation. Expression analyses showed that OsAGO17 was highly expressed in young panicles and nodes, which was consistent with the expression pattern of OsmiR397b. SRNA sequencing, stem‐loop RT‐PCR and sRNA blotting showed that the expression of OsmiR397b was reduced in ago17 and enhanced in the OsAGO17 OE lines. Four OsmiR397b target laccase (LAC) genes showed complementary expression patterns with OsAGO17 and OsmiR397b. Combined with the results of immunoprecipitation (IP) analysis, we suggested that OsAGO17 formed an RISC with OsmiR397b and affected rice development by suppression of LAC expression. In conclusion, OsAGO17 might be a critical protein in the sRNA pathway and positively regulates grain size and weight in rice.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

A putative AGO protein, OsAGO17, positively regulates grain size and grain weight through OsmiR397b in rice

Zhong

Zhu

et al. 2019

Plant Biotechnology Journal

View full text Add to dashboard Cite

show abstract

“…OsLAC13 regulated the seed setting rate in rice by suppressing the transport of sugars to the anthers and promoting H 2 O 2 production through unknown mechanisms (Yu et al, 2017). However, heterologous expression of OsLAC10 in Arabidopsis plants increased lignification around vasculature and increased Cu stress tolerance (Liu et al, 2017). Triple mutant of atlac4, atlac11 and atlac17 had very much reduced lignin deposition in the vasculature and the plants were dwarf (Zhao et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

Major Domestication-Related Phenotypes inIndicaRice Are Due to Loss of miRNA-Mediated Laccase Silencing

et al. 2018

View full text Add to dashboard Cite

Domestication of rice (Oryza sativa) included conversion of perennial wild species with few seeds to short plants that produced abundant seeds. Most domestication-associated changes were due to variations in transcription factors and other key proteins such as enzymes. Here, we show that multiple yield-related traits associated with indica rice domestication are linked to micro (mi) RNA-mediated regulation. Analysis of small (s) RNA data sets from cultivated indica rice lines, a few landraces, and two wild relatives of rice revealed the presence of abundant 22-nucleotide (nt) reads in wild relatives that mapped to miR397 precursors. miR397 was expressed at very high levels in wild relatives and at negligible levels in high-yielding cultivated lines. In its genera-specific form of 22-nt, miR397 targeted mRNAs encoding laccases that decayed and induced robust secondary cascade silencing in wild species that required RNA-dependent RNA polymerase 6. In wild species of rice, reduced expression of laccases resulted in low lignification. As expected, overexpression of miR397 induced de-domestication phenotypes. At least 26 uncharacterized QTLs previously implicated in rice yield overlapped with laccases and miR397 genes. These results suggest that miRNAs contribute to rice domestication-associated phenotypes.

show abstract

“…Based on the fast reddish-brown color formation, indicating oxidation of guaiacol ( Figure 1A), as well as the best activity of cell-free extracts in ABTS assay ( Figure 1B), three strains, namely P. putida Catalysts 2019, 9,629 3 of 14 F6, P. putida KT2440, and P. putida CA-3, were chosen for further study. Notably, cell-free extracts of P. putida F6 exhibited two times higher laccase activity (ABTS assay) compared to cell free extracts from P. putida KT2440 and P. putida CA-3, respectively, which showed a similar activity level ( Figure 1B).…”

Section: Screening For Laccase Activity Using Guaiacol Agar Plates Anmentioning

confidence: 99%

“…Laccases are blue multicopper enzymes (EC 1.10.3.2) that oxidize a broad range of both phenolic and non-phenolic substrates, via a four-electron reduction of molecular oxygen to water [1,2]. These enzymes are widely distributed in nature and have been isolated from bacteria [3][4][5], fungi [6,7] and plants [8,9], as well as from lichens [10], and sponges [11]. Although laccases are heterogeneous in different species, implying diversity in their function, four copper-binding motifs are conserved in the…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes

et al. 2019

View full text Add to dashboard Cite

Laccases are multicopper-oxidases with variety of biotechnological applications. While predominantly used, fungal laccases have limitations such as narrow pH and temperature range and their production via heterologous protein expression is more complex due to posttranslational modifications. In comparison, bacterial enzymes, including laccases, usually possess higher thermal and pH stability, and are more suitable for expression and genetic manipulations in bacterial expression hosts. Therefore, the aim of this study was to identify, recombinantly express, and characterize novel laccases from Pseudomonas spp. A combination of approaches including DNA sequence analysis, N-terminal protein sequencing, and genome sequencing data analysis for laccase amplification, cloning, and overexpression have been used. Four active recombinant laccases were obtained, one each from P. putida KT2440 and P. putida CA-3, and two from P. putida F6. The new laccases exhibited broad temperature and pH range and high thermal stability, as well as the potential to degrade selection of synthetic textile dyes. The best performing laccase was CopA from P. putida F6 which degraded five out of seven tested dyes, including Amido Black 10B, Brom Cresol Purple, Evans Blue, Reactive Black 5, and Remazol Brilliant Blue. This work highlighted species of Pseudomonas genus as still being good sources of biocatalytically relevant enzymes. most laccases, especially bacterial forms [12]. The presence of different metal ions can affect laccase activity, either inducing or suppressing it. Metal ions such as Cu +2 , Ca +2 , Ni +2 , Co +2 , and Mn +2 are generally known to accelerate laccase activity at a remarkable level [13].Due to broad substrate spectrum, laccases have become very attractive for a variety of biotechnological and industrial applications such as organic synthesis; lignin degradation; and bio-product formation for the food, textile, and pharmaceutical industries; remediation of contaminated environments; as well as construction of biosensors and biofuel cells [14][15][16]. During the last decade laccases have been used in decolorization and detoxification of textile effluents [17]. Effluents from the textile industry are usually complex, containing a wide variety of synthetic dyes [18], among which the most common are azo dyes, anthraquinone, triphenylmethane, and indigo dyes [19].In the recent years, development of high-performance recombinant bacterial strains and the possibility of increasing the production of recombinant proteins created new opportunities for the commercial use of laccases, since the production from wild type strains has limitations in growth and product yield, which are not suitable for standard industrial fermentations [20]. The majority of studies on laccases are focused on laccases originated from fungi. Having in mind that industrial processes often require high temperature and pressure, or extremely acidic or alkaline pH, fungal laccases are not the best candidates for such industrial applications since they oper...

show abstract

Comprehensive Analysis of Rice Laccase Gene (OsLAC) Family and Ectopic Expression of OsLAC10 Enhances Tolerance to Copper Stress in Arabidopsis

Cited by 115 publications

References 55 publications

A putative AGO protein, OsAGO17, positively regulates grain size and grain weight through OsmiR397b in rice

A putative AGO protein, OsAGO17, positively regulates grain size and grain weight through OsmiR397b in rice

Major Domestication-Related Phenotypes inIndicaRice Are Due to Loss of miRNA-Mediated Laccase Silencing

Identification and Characterization of New Laccase Biocatalysts from Pseudomonas Species Suitable for Degradation of Synthetic Textile Dyes

Contact Info

Product

Resources

About