植物学报
植物學報
식물학보
ACTA BOTANICA SINICA
2004年
6期
751-756
,共6页
赵虎基%王建华%高鹏%顾日良%张京强%王天宇%王国英
趙虎基%王建華%高鵬%顧日良%張京彊%王天宇%王國英
조호기%왕건화%고붕%고일량%장경강%왕천우%왕국영
谷子%乙酰辅酶A羧化酶%克隆%抗除草剂%靶位点
穀子%乙酰輔酶A羧化酶%剋隆%抗除草劑%靶位點
곡자%을선보매A최화매%극륭%항제초제%파위점
Setaria italica%Acetyl-CoA Carboxylase%cloning%,herbicide%target site
乙酰辅酶A羧化酶是一个生物素羧化酶,它所催化的反应是脂肪酸生物合成中的第一个植物叶绿体中的乙酰辅酶A羧化酶是两类禾本科除草剂的靶蛋白.从抗除草剂拿捕净和感拿捕净的谷子(SetariaitalicaBeauv.)中克隆了两个乙酰辅酶A羧化酶的全长cDNA,分别命名为foxACC-R和foxACC-S,它们推导的蛋白质均编码2 321个氨基酸,然而在第1 780个氨基酸处,foxACC-R编码亮氨酸,而foxACC-S编码异亮氨酸.采用生物信息学方法,我们推断这个cDNA编码的是叶绿体中的乙酰辅酶A羧化酶,并预测了它的功能域和保守区.通过这两个cDNA编码的氨基酸序列与其他乙酰辅酶A羧化酶的序列比较得出结论,亮氨酸/异亮氨酸位点可能是APPs和CHDs两类除草剂作用的关键位点.Southern杂交分析的结果显示,该基因在谷子基因组中只有一个拷贝.
乙酰輔酶A羧化酶是一箇生物素羧化酶,它所催化的反應是脂肪痠生物閤成中的第一箇植物葉綠體中的乙酰輔酶A羧化酶是兩類禾本科除草劑的靶蛋白.從抗除草劑拿捕淨和感拿捕淨的穀子(SetariaitalicaBeauv.)中剋隆瞭兩箇乙酰輔酶A羧化酶的全長cDNA,分彆命名為foxACC-R和foxACC-S,它們推導的蛋白質均編碼2 321箇氨基痠,然而在第1 780箇氨基痠處,foxACC-R編碼亮氨痠,而foxACC-S編碼異亮氨痠.採用生物信息學方法,我們推斷這箇cDNA編碼的是葉綠體中的乙酰輔酶A羧化酶,併預測瞭它的功能域和保守區.通過這兩箇cDNA編碼的氨基痠序列與其他乙酰輔酶A羧化酶的序列比較得齣結論,亮氨痠/異亮氨痠位點可能是APPs和CHDs兩類除草劑作用的關鍵位點.Southern雜交分析的結果顯示,該基因在穀子基因組中隻有一箇拷貝.
을선보매A최화매시일개생물소최화매,타소최화적반응시지방산생물합성중적제일개식물협록체중적을선보매A최화매시량류화본과제초제적파단백.종항제초제나포정화감나포정적곡자(SetariaitalicaBeauv.)중극륭료량개을선보매A최화매적전장cDNA,분별명명위foxACC-R화foxACC-S,타문추도적단백질균편마2 321개안기산,연이재제1 780개안기산처,foxACC-R편마량안산,이foxACC-S편마이량안산.채용생물신식학방법,아문추단저개cDNA편마적시협록체중적을선보매A최화매,병예측료타적공능역화보수구.통과저량개cDNA편마적안기산서렬여기타을선보매A최화매적서렬비교득출결론,량안산/이량안산위점가능시APPs화CHDs량류제초제작용적관건위점.Southern잡교분석적결과현시,해기인재곡자기인조중지유일개고패.
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-R and foxACC-S, have been cloned. cDNA sequencing showed that they encode a protein of 2 321 amino acids long with a pl 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-Rother than Ile in fox4CC-Sand other cereal plastid ACCase. It is suspected that the change of Ile 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.