云南植物研究
雲南植物研究
운남식물연구
ACTA BOTANICA YUNNANICA
2009年
5期
433-438
,共6页
杨明挚%黄兴奇%张汉波%陈善娜%杨红玉%程在全
楊明摯%黃興奇%張漢波%陳善娜%楊紅玉%程在全
양명지%황흥기%장한파%진선나%양홍옥%정재전
稻属%丝氨酸/苏氨酸蛋白激酶基因%保守性分析%转录分析
稻屬%絲氨痠/囌氨痠蛋白激酶基因%保守性分析%轉錄分析
도속%사안산/소안산단백격매기인%보수성분석%전록분석
Oryza%Serine/thronine protein kinase gene (OsSTK)%Conservation analysis%Transcription analysis
从水稻中克隆了一个在稻属植物中高度保守和组成型表达的丝氨酸/苏氨酸蛋白激酶基因(OsSTK).该基因包含两个外显子和一个114 bp的小内含子序列,预测编码一个419个氨基酸的蛋白质.该基因推导的氨基酸序列与其它已知序列的一致性均低于52%.利用从不同种和类型的野生稻克隆的部分该基因序列构建的系统树与野生稻的分类和进化关系相一致.OSPK N-端拥有一段富含丝氨酸、碱性氨基酸和带电荷氨基酸的特异性导肽序列,其中包含"GDGDGDGDG"短重复序列.由于该基因蛋白激酶结构域中的Vib, VⅢ和XI亚结构域中同时具有酪氨酸蛋白激酶和丝氨酸/苏氨酸蛋白激酶的特性,推测该基因可能同时具有催化酪氨酸和丝氨酸、苏氨酸磷酸化的双重功能.
從水稻中剋隆瞭一箇在稻屬植物中高度保守和組成型錶達的絲氨痠/囌氨痠蛋白激酶基因(OsSTK).該基因包含兩箇外顯子和一箇114 bp的小內含子序列,預測編碼一箇419箇氨基痠的蛋白質.該基因推導的氨基痠序列與其它已知序列的一緻性均低于52%.利用從不同種和類型的野生稻剋隆的部分該基因序列構建的繫統樹與野生稻的分類和進化關繫相一緻.OSPK N-耑擁有一段富含絲氨痠、堿性氨基痠和帶電荷氨基痠的特異性導肽序列,其中包含"GDGDGDGDG"短重複序列.由于該基因蛋白激酶結構域中的Vib, VⅢ和XI亞結構域中同時具有酪氨痠蛋白激酶和絲氨痠/囌氨痠蛋白激酶的特性,推測該基因可能同時具有催化酪氨痠和絲氨痠、囌氨痠燐痠化的雙重功能.
종수도중극륭료일개재도속식물중고도보수화조성형표체적사안산/소안산단백격매기인(OsSTK).해기인포함량개외현자화일개114 bp적소내함자서렬,예측편마일개419개안기산적단백질.해기인추도적안기산서렬여기타이지서렬적일치성균저우52%.이용종불동충화류형적야생도극륭적부분해기인서렬구건적계통수여야생도적분류화진화관계상일치.OSPK N-단옹유일단부함사안산、감성안기산화대전하안기산적특이성도태서렬,기중포함"GDGDGDGDG"단중복서렬.유우해기인단백격매결구역중적Vib, VⅢ화XI아결구역중동시구유락안산단백격매화사안산/소안산단백격매적특성,추측해기인가능동시구유최화락안산화사안산、소안산린산화적쌍중공능.
A cytoplasmic serine/thronine protein kinase gene (OsSTK), had been cloned from Oryza genus. It was found high conservative and constitutive expression in Oryza. OsSTK gene had two exons, separated by 114 bp short intron. The open reading frame of OsSTK gene that predicted encoded a 419 amino acids protein. The amino acid sequence of OsSTK had low identities (less than 53%) with any other known protein kinase. The phylogenetic tree based on the partial DNA sequences of OsSTK from different species and types of wild rice and cultivated rice, was close to the taxation system of rice. Interestingly, OsSTK had a serine, including basic amino acids and charged amino acids abundant polypeptide with a "GDGDGDGDG" sequence at N-terminal that had not been found in any other genes. OsSTK may play dual specificity that phosphorylates both serine/thronine and tyrosone, because the amino acids module of Vib, VⅢ and XI catalytic domain have both the serine/thronine and tyrosine kinase characters.