Cloning of Plastid Acetyl-CoA Carboxylase cDNA from Setaria italica and Sequence Analysis of Graminicide Target Site
文献类型: 外文期刊
第一作者: Zhao, HJ
作者: Zhao, HJ;Wang, JH;Gao, P;Gu, RL;Zhang, JQ;Wang, TY;Wang, GY
作者机构:
关键词: setaria italica;acetyl-CoA carboxylase;cloning;herbicide;target site
期刊名称:ACTA BOTANICA SINICA ( 影响因子:0.599; )
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年卷期:
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收录情况: SCI
摘要: Acetyl-CoA carboxylase (ACCase) is a biotinylated enzyme that catalyzes the first committed step in fatty acid biosynthesis. Graminaceous ACCase in plastid is the target site of two classes of graminicide herbicides. Two full-length cDNAs of plastid ACCase from sethoxydim-resistant and sensitive Setaria italica Beauv., named foxACC-Rand foxACC-S, have been cloned. cDNA sequencing showed that they encode a protein of 2 321 amino acids long with a pi of 5.89 and a calculated molecular mass of 256 kD. The sequences of foxACC-Rand foxACC-Shave been compared with their homologs from other plants and analyzed for conserved amino acid regions and their functional domains. It is found that the amino acid at position 1 780 is Leu in foxACC-R other than He in fox ACC-S and other cereal plastid ACCase. It is suspected that the change of He to Leu residue is critical for interaction of plastid ACCase with cereal herbicides APPs and CHDs. According to Southern hybridization, foxACC-R and foxACC-S are both estimated to be single copy in the genome of S. italica.
分类号: Q94
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