Over-expression of CYP78A98, a cytochrome P450 gene from Jatropha curcas L., increases seed size of transgenic tobacco

Yinshuai Tian,Fang Chen,Jiao Dai,Min Zhang,Xiaole Hu,Linghui Wang,Ying Xu

doi:10.1016/j.ejbt.2015.11.001

Abstract

Background: Jatropha curcas L. (further referred to as Jatropha ), as a rapidly emerging biofuel crop, has attracted worldwide interest. However, Jatropha is still an undomesticated plant, the true potential of this shrub has not yet been fully realized. To explore the potential of Jatropha , breeding and domestication are needed. Seed size is one of the most important traits of seed yield and has been selected since the beginning of agriculture. Increasing the seed size is a main goal of Jatropha domestication for increasing the seed yield, but the genetic regulation of seed size in Jatropha has not been fully understood. Results: We cloned CYP78A98 gene from Jatropha , a homologue of CYP78A5 in Arabidopsis . We found that CYP78A98 was highly expressed in male flower, female flower, stem apex, leaf and developing seed. However, its transcripts were hardly detected in root and stem. CYP78A98 protein localized in endoplasmic reticulum (ER) and the hydrophobic domain at the N-terminus was essential for the correct protein localization. Furthermore, INNER NO OUTER promoter (pINO) drove specific overexpression of CYP78A98 in transgenic tobacco seeds resulted in increased seed size and weight, as well as improved seed protein and fatty acid content. Conclusions: The results indicated that CYP78A98 played a role in Jatropha seed size control. This may help us to better understand the genetic regulation of Jatropha seed development, and accelerate the breeding progress of Jatropha .

Highlights

Lignocellulosic biomass, the most abundant biomass on earth, has a great potential as renewable feedstock for biorefinery processes including biofuel production
This study focused on the isolation of cellulase producing bacteria from soil sample obtained from the local rice paddy fields in Thailand
The crude cellulase enzymes collected from supernatant fractions of 5 bacterial isolates were mixed with 2 types of cellulose substrates, filter paper (FP) and CMC

Summary

Introduction

Lignocellulosic biomass, the most abundant biomass on earth, has a great potential as renewable feedstock for biorefinery processes including biofuel production. It mainly comprises of three components including cellulose, hemicelluloses and lignin [1]. To overcome the recalcitrance of lignocellulosic biomass, it needs the promising pretreatment method to promote enzyme accessibility to substrate and highly efficient hydrolysis to produce fermentable sugars. The optimum temperature and pH of the enzyme is 50°C and pH 6.0, respectively This cellulase retained its activity more than 90% at 55°C, and pH 4.0. Conclusion: The characterization of cellulase produced from MSL2 strain was described here These properties of cellulase made this bacterial strain become potential to be used in the biorefining process

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