生物学杂志
生物學雜誌
생물학잡지
JOURNAL OF BIOLOGY
2014年
5期
55-59
,共5页
王玮蔚%王冬梅%沈佳%孙雪
王瑋蔚%王鼕梅%瀋佳%孫雪
왕위위%왕동매%침가%손설
蛋白核小球藻%碳酸酐酶%生物信息学分析
蛋白覈小毬藻%碳痠酐酶%生物信息學分析
단백핵소구조%탄산항매%생물신식학분석
Chlorella pyrenoidosa%carbonic anhydrase%bioinformatics analysis
选取蛋白核小球藻( Chlorella pyrenoidosa)中不同碳酸酐酶亚型(α-CA、β-CA、γ-CA)基因,对其编码蛋白的理化性质、跨膜结构域、信号肽及蛋白高级结构进行了分析和预测。结果表明蛋白核小球藻α-CA、β-CA和γ-CA蛋白分子量分别为28.9 kDa、34.9 kDa和24.8 kDa,均为酸性、微亲水和脂溶性蛋白。α-CA可以检测到强的跨膜结构和信号肽区域,推测为胞外CA。β-CA和γ-CA无可信的跨膜结构域和信号肽区域,推测β-CA可能位于细胞质或叶绿体基质中,而γ-CA位于线粒体基质中。 CA蛋白的二级结构预测结果表明α-CA中无规则卷曲所占百分比最高(64.66%),β-CA中α螺旋和无规则卷曲所占百分比分别为44.76%和44.13%,而γ-CA中α螺旋和无规则卷曲含量分别为39.48%和40.34%。三级结构预测分析表明α-CA折叠较松散,β-CA、γ-CA折叠程度较紧密,且γ-CA具有反复折叠的结构。
選取蛋白覈小毬藻( Chlorella pyrenoidosa)中不同碳痠酐酶亞型(α-CA、β-CA、γ-CA)基因,對其編碼蛋白的理化性質、跨膜結構域、信號肽及蛋白高級結構進行瞭分析和預測。結果錶明蛋白覈小毬藻α-CA、β-CA和γ-CA蛋白分子量分彆為28.9 kDa、34.9 kDa和24.8 kDa,均為痠性、微親水和脂溶性蛋白。α-CA可以檢測到彊的跨膜結構和信號肽區域,推測為胞外CA。β-CA和γ-CA無可信的跨膜結構域和信號肽區域,推測β-CA可能位于細胞質或葉綠體基質中,而γ-CA位于線粒體基質中。 CA蛋白的二級結構預測結果錶明α-CA中無規則捲麯所佔百分比最高(64.66%),β-CA中α螺鏇和無規則捲麯所佔百分比分彆為44.76%和44.13%,而γ-CA中α螺鏇和無規則捲麯含量分彆為39.48%和40.34%。三級結構預測分析錶明α-CA摺疊較鬆散,β-CA、γ-CA摺疊程度較緊密,且γ-CA具有反複摺疊的結構。
선취단백핵소구조( Chlorella pyrenoidosa)중불동탄산항매아형(α-CA、β-CA、γ-CA)기인,대기편마단백적이화성질、과막결구역、신호태급단백고급결구진행료분석화예측。결과표명단백핵소구조α-CA、β-CA화γ-CA단백분자량분별위28.9 kDa、34.9 kDa화24.8 kDa,균위산성、미친수화지용성단백。α-CA가이검측도강적과막결구화신호태구역,추측위포외CA。β-CA화γ-CA무가신적과막결구역화신호태구역,추측β-CA가능위우세포질혹협록체기질중,이γ-CA위우선립체기질중。 CA단백적이급결구예측결과표명α-CA중무규칙권곡소점백분비최고(64.66%),β-CA중α라선화무규칙권곡소점백분비분별위44.76%화44.13%,이γ-CA중α라선화무규칙권곡함량분별위39.48%화40.34%。삼급결구예측분석표명α-CA절첩교송산,β-CA、γ-CA절첩정도교긴밀,차γ-CA구유반복절첩적결구。
In this paper, three kinds of CA genes like(α-CA, β-CA and γ-CA) were selected from Chlorella pyrenoidosa, and the physical and chemical properties, transmembrane domain, signal peptide, secondary and tertiary structures of CA isoforms were predic-ted through bioinformatics tools.The results showed that the molecular weights ofα-CA,β-CA and γ-CA were 28.9 kDa, 34.9 kDa and 24.8 kDa, respectively.And they were all acidic, slightly hydrophilic and fat-soluble proteins.One signal peptide and a strong transmembrane domain were detected inα-CA, soα-CA was presumed an extracellular CA.There were no credible transmembrane re-gions and signal peptides in theβ-CA and γ-CA sequences.Combined with the subcellular localization results,β-CA might locate in the cytoplasm or chloroplast stroma, whileγ-CA was in the mitochondrial stroma.The results of secondary structure prediction showed that the percentage of random coil inα-CA was highest, which occupied 64.66%.And the proportions ofα-helix and random coil were almost the same as inβ-CA, which were 44.76%and 44.13%, respectively.And the proportions ofα-helix and random coil inγ-CA protein accounted for 39.48%and 40.34%, respectively.The tertiary structure prediction showed that three dimensional structure ofα-CA was loose,β-CA,γ-CA were relatively compact, and theγ-CA was found to hare a repeated folding-structure.