Ubiquitin ligase gene OsNLA2, protein and application of ubiquitin ligase gene OsNLA2 in rice selection

Abstract

The invention discloses a ubiquitin ligase gene OsNLA2, a protein and application of the ubiquitin ligase gene OsNLA2 in rice selection. The protein encoded by the ubiquitin ligase gene OsNLA2 has anamino acid sequence shown as SEQ ID NO. 1, and a cDNA sequence shown as SEQ ID NO. 2. Through construction of rice plants with gene OsNLA2 expression and rice plants with gene OsNLA2 mutation, it is found that gene OsNLA2 expression can be improved so as to have grain sizes and 1000-grain weights of normal rice grains increased; and moreover, rice plant heights in low-nitrogen environment can alsobe increased. In addition, the gene OsNLA2 expression can be knocked-out so as to have quantities and weights of normal individual rice plants increased. Therefore, the gene OsNLA2 can be used for improving rice grain types, 1000-grain weights and rice plant heights in low-nitrogen environment in the process of rice selection; and moreover, the gene OsNLA2 can also be used for improving rice yield in the process of rice selection. In addition, the gene OsNLA2 is also of important application values in the aspects of plant seed size, weight, yield, low-nitrogen-environment plant height increase and the like.

Description

technical field [0001] The invention belongs to the field of plant genetic engineering, and specifically refers to an ubiquitin ligase gene OsNLA2, a protein and its application in rice breeding. Background technique [0002] Ubiquitination is a type of protein post-translational modification, which is involved in many aspects of plant stress and growth and development. The ubiquitination process involves ubiquitin ligases, ubiquitin activating enzymes and ubiquitin conjugating enzymes. E3 ubiquitin ligase plays a very important role in the ubiquitination pathway, which is responsible for the specific recognition of protein substrates and the recruitment and transport of 76 amino acid ubiquitin molecules to lysine residues of protein substrates ( Deshaies R J, Joazeiro C A. RING domain E3ubiquitin ligases [J]. Annual Review of Biochemistry, 2009, 78(1): 399-434.). E3 ubiquitin ligases determine the specificity of ubiquitinated substrates, and the RING type plays an importa...

Images