分子植物育种
分子植物育種
분자식물육충
MOLECULAR PLANT BREEDING
2013年
5期
571-577
,共7页
黄琼林%梁凌玲%何瑞%詹若挺%陈蔚文
黃瓊林%樑凌玲%何瑞%詹若挺%陳蔚文
황경림%량릉령%하서%첨약정%진위문
青天葵%EBP1基因%克隆%分析
青天葵%EBP1基因%剋隆%分析
청천규%EBP1기인%극륭%분석
Nervilia fordii (Hance) schltr%EBP1%Cloning%Analysis
表皮生长因子受体3结合蛋白(ErbB3 binding protein, EBP1)是植物器官大小生长的关键调控因子。本研究应用RACE-PCR技术从濒危药用植物青天葵(Nevilia fordii (Hance) Schltr.)中克隆获得EBP1编码基因并命名为NfEBP1。该基因全长为1188 bp (Genbank登记号JN854245),编码395个氨基酸。生物信息学分析表明,NfEBP1蛋白分子量为43.4 kD,等电点为6.12,整体表现为亲水性。NfEBP1不含信号肽、叶绿体转运肽或线粒体靶向肽,整体位于细胞膜外;其二级结构由21个α-螺旋、21个延伸链、18个β-转角和28个随意卷曲构成。 NfEBP1含有PA2G4细胞增殖功能域,与其他植物EBP1有着高度的同源性,均归属APP_MetAP超级家族。 NfEBP1在青天葵不同组织均有表达,相对表达量以叶片最高,球茎次之,叶柄则最低。本研究成功克隆青天葵EBP1基因并分析其在青天葵不同组织的表达水平,为下一步利用该基因促进青天葵器官生长研究提供了基础数据。
錶皮生長因子受體3結閤蛋白(ErbB3 binding protein, EBP1)是植物器官大小生長的關鍵調控因子。本研究應用RACE-PCR技術從瀕危藥用植物青天葵(Nevilia fordii (Hance) Schltr.)中剋隆穫得EBP1編碼基因併命名為NfEBP1。該基因全長為1188 bp (Genbank登記號JN854245),編碼395箇氨基痠。生物信息學分析錶明,NfEBP1蛋白分子量為43.4 kD,等電點為6.12,整體錶現為親水性。NfEBP1不含信號肽、葉綠體轉運肽或線粒體靶嚮肽,整體位于細胞膜外;其二級結構由21箇α-螺鏇、21箇延伸鏈、18箇β-轉角和28箇隨意捲麯構成。 NfEBP1含有PA2G4細胞增殖功能域,與其他植物EBP1有著高度的同源性,均歸屬APP_MetAP超級傢族。 NfEBP1在青天葵不同組織均有錶達,相對錶達量以葉片最高,毬莖次之,葉柄則最低。本研究成功剋隆青天葵EBP1基因併分析其在青天葵不同組織的錶達水平,為下一步利用該基因促進青天葵器官生長研究提供瞭基礎數據。
표피생장인자수체3결합단백(ErbB3 binding protein, EBP1)시식물기관대소생장적관건조공인자。본연구응용RACE-PCR기술종빈위약용식물청천규(Nevilia fordii (Hance) Schltr.)중극륭획득EBP1편마기인병명명위NfEBP1。해기인전장위1188 bp (Genbank등기호JN854245),편마395개안기산。생물신식학분석표명,NfEBP1단백분자량위43.4 kD,등전점위6.12,정체표현위친수성。NfEBP1불함신호태、협록체전운태혹선립체파향태,정체위우세포막외;기이급결구유21개α-라선、21개연신련、18개β-전각화28개수의권곡구성。 NfEBP1함유PA2G4세포증식공능역,여기타식물EBP1유착고도적동원성,균귀속APP_MetAP초급가족。 NfEBP1재청천규불동조직균유표체,상대표체량이협편최고,구경차지,협병칙최저。본연구성공극륭청천규EBP1기인병분석기재청천규불동조직적표체수평,위하일보이용해기인촉진청천규기관생장연구제공료기출수거。
ErbB3 binding protein is a key regulator of organ size in plants. An EBP1 gene was cloned from N. fordii by RACE-PCR and named as NfEBP1 (Genbank accession number JN854245). The ORF of NfEBP1 cont-ained 1 188 base pairs encoding 395 amino acids. The molecular weight of NfEBP1 protein was 43.5 kD, the isoelectric point was 6.12, and its overall structure exhibited hydrophilic. NfEBP1 contains no signal peptide , chloroplast transit peptide, mitochondrial targeting peptide, and located entirely outside cell membrane. The predicted secondary structure of NfEBP1 was composed of 21α-helixes, 21 extend strands, 18β-turners and 28 random coils. NfEBP1 showed high homology with EBP1 protein from other plants, and possessed a functional domain PA2G4. NfEPB1 was ubiquitously expressed in all tissues of N. fordii, and the relative expression level reached the highest in leaf, and the lowest in petiole. This study provided a firmfoundation for promoting organ size of N. fordii by manipulating EBP1.