白念珠菌CaPTC6和CaHXT5基因及酿酒酵母ScATP16基因的功能研究
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摘要
蛋白质的可逆磷酸化是真核细胞信号转导途径中的一个关键调控机制,蛋白磷酸酯酶是这一可逆过程中的关键酶,PP2C是依赖于镁离子或锰离子的单体蛋白磷酸酯酶。葡萄糖是大多数生物的主要能量来源,涉及到许多生物学过程。白念珠菌是一种重要的机会性致病真菌。白念珠菌表现出多种形态特征,与它能够利用多种糖类作为碳源密切相关。为了挖掘抗真菌药物的作用靶点,我们首先对参与蛋白质可逆磷酸化的PP2C基因CaPTC6和参与葡萄糖转运的CaHXT5基因的功能进行了研究。
通过酿酒酵母和白念珠菌数据库的搜索比对,我们获得了白念珠菌基因CaPTC6和CaHXT5的序列。CaPTC6的ORF长为1299bp,编码433个氨基酸,CaPTC6与ScPTC6所编码蛋白氨基酸序列的相似性为26.9%。我们克隆并在细菌中表达了CaPtc6p的催化区域,发现重组蛋白具有去磷酸化活性,这种活性依赖于Mg2+或Mn2+的存在,并且受到丝氨酸/苏氨酸去磷酸酯酶抑制剂NaF的抑制,表明CaPtc6p是一种PP2C类蛋白磷酸酯酶。我们采用URA-BLASTER方法依次敲除了CaPTC6两个等位基因,但是没有发现该基因缺失株的任何表型。
CaHXT5基因的ORF长1836bp,编码612个氨基酸,CaHXT5与酿酒酵母ScHXT5所编码的氨基酸序列相似性为28%。我们应用同样策略构建了Cahxt5缺失菌株并用PCR方法证实了其基因型。但是,表型研究发现CaHXT5基因的缺失并没有影响白念珠菌细胞对于糖类的利用,也没有影响细胞的菌丝形成能力。我们推测白念珠菌中葡萄糖转运蛋白家族中其他成员可能起着重要的代偿作用。
最近研究表明酵母细胞ATP合酶的δ亚基上的一个丝氨酸残基可以被磷酸化,这表明δ亚基的功能是受蛋白磷酸化所调控的。为了深入研究δ亚基的磷酸化调控机理,我们功能性表达了酿酒酵母线粒体ATP合酶组分δ亚基并制备了针对这一亚基的多克隆抗体,采用定点突变技术,构建了δ亚基磷酸化位点的突变体。但是,发现δ亚基的磷酸化并不影响线粒体ATP合酶在细胞利用非发酵性碳源方面的功能。
Candida albicans is the importantly opportunitive fungal pathogen. The type 2C protein phosphatases are one group of serine/threonine protein phosphatases involved in the reversible protein phosphorylation. Glucose is the major source of energy in cells and involved in many cellular processes. To identify potential drug target genes in the most important human fungal pathogen C. albicans, we chose to study the functions of CaPTC6 and CaHXT5 genes.
From the Candida genome database, we identified CaPTC6 and CaHXT5 gene sequences. CaPTC6 has an open reading frame (ORF) of 1299bp in length, which encodes a protein of 433 amino acids sharing 26.9% similarity with ScPtc6p at amino acid level. We cloned and expressed the catalytic domain of CaPtc6p, and found that the purified catalytic domain protein exhibited dephosphorylation activity, which was dependent on the presence of Mg2+ or Mn2+ ion and inhibited by the protein Ser/Thr phosphatase inhibitor NaF. These results indicate that CaPTC6 encoded a PP2C phosphatase. We constructed the homozygous deletion mutant for CaPTC6, but did not find any phenotype for this mutant under various growth conditions.
CaHXT5 has an ORF of 1836bp, which encodes a protein of 612 amino acids sharing 28% similarity with ScHxt5p at the amino acid level. We constructed the homozygous mutant of CaHXT5. However, the homozygous mutant did not show any visible phenotype in utilization of different sugars and in hypha formation. We speculate that other members of glucose transporters might play a redundant role for CaHxt5p in these processes.
Recent studies show that the ScATP16-encodedδsubunit of the mitochondrial F1F0-ATP synthase is phosphorylated in Saccharomyces cerevisia. To understand the molecular mechanism by which the phosphorylation of the delta subunit is regulated. We expressed aδ-His6 fusion protein in bacterial cells and prepared its rabbit polyclonal antibodies. In addition, we applied site-directed mutagenesis to construct the point mutant at the phosphorylation site of theδsubunit. However, we found that this mutation does not affect the function of mitochondrial ATP synthase in the utilization of nonfermentable carbon sources.
通过酿酒酵母和白念珠菌数据库的搜索比对,我们获得了白念珠菌基因CaPTC6和CaHXT5的序列。CaPTC6的ORF长为1299bp,编码433个氨基酸,CaPTC6与ScPTC6所编码蛋白氨基酸序列的相似性为26.9%。我们克隆并在细菌中表达了CaPtc6p的催化区域,发现重组蛋白具有去磷酸化活性,这种活性依赖于Mg2+或Mn2+的存在,并且受到丝氨酸/苏氨酸去磷酸酯酶抑制剂NaF的抑制,表明CaPtc6p是一种PP2C类蛋白磷酸酯酶。我们采用URA-BLASTER方法依次敲除了CaPTC6两个等位基因,但是没有发现该基因缺失株的任何表型。
CaHXT5基因的ORF长1836bp,编码612个氨基酸,CaHXT5与酿酒酵母ScHXT5所编码的氨基酸序列相似性为28%。我们应用同样策略构建了Cahxt5缺失菌株并用PCR方法证实了其基因型。但是,表型研究发现CaHXT5基因的缺失并没有影响白念珠菌细胞对于糖类的利用,也没有影响细胞的菌丝形成能力。我们推测白念珠菌中葡萄糖转运蛋白家族中其他成员可能起着重要的代偿作用。
最近研究表明酵母细胞ATP合酶的δ亚基上的一个丝氨酸残基可以被磷酸化,这表明δ亚基的功能是受蛋白磷酸化所调控的。为了深入研究δ亚基的磷酸化调控机理,我们功能性表达了酿酒酵母线粒体ATP合酶组分δ亚基并制备了针对这一亚基的多克隆抗体,采用定点突变技术,构建了δ亚基磷酸化位点的突变体。但是,发现δ亚基的磷酸化并不影响线粒体ATP合酶在细胞利用非发酵性碳源方面的功能。
Candida albicans is the importantly opportunitive fungal pathogen. The type 2C protein phosphatases are one group of serine/threonine protein phosphatases involved in the reversible protein phosphorylation. Glucose is the major source of energy in cells and involved in many cellular processes. To identify potential drug target genes in the most important human fungal pathogen C. albicans, we chose to study the functions of CaPTC6 and CaHXT5 genes.
From the Candida genome database, we identified CaPTC6 and CaHXT5 gene sequences. CaPTC6 has an open reading frame (ORF) of 1299bp in length, which encodes a protein of 433 amino acids sharing 26.9% similarity with ScPtc6p at amino acid level. We cloned and expressed the catalytic domain of CaPtc6p, and found that the purified catalytic domain protein exhibited dephosphorylation activity, which was dependent on the presence of Mg2+ or Mn2+ ion and inhibited by the protein Ser/Thr phosphatase inhibitor NaF. These results indicate that CaPTC6 encoded a PP2C phosphatase. We constructed the homozygous deletion mutant for CaPTC6, but did not find any phenotype for this mutant under various growth conditions.
CaHXT5 has an ORF of 1836bp, which encodes a protein of 612 amino acids sharing 28% similarity with ScHxt5p at the amino acid level. We constructed the homozygous mutant of CaHXT5. However, the homozygous mutant did not show any visible phenotype in utilization of different sugars and in hypha formation. We speculate that other members of glucose transporters might play a redundant role for CaHxt5p in these processes.
Recent studies show that the ScATP16-encodedδsubunit of the mitochondrial F1F0-ATP synthase is phosphorylated in Saccharomyces cerevisia. To understand the molecular mechanism by which the phosphorylation of the delta subunit is regulated. We expressed aδ-His6 fusion protein in bacterial cells and prepared its rabbit polyclonal antibodies. In addition, we applied site-directed mutagenesis to construct the point mutant at the phosphorylation site of theδsubunit. However, we found that this mutation does not affect the function of mitochondrial ATP synthase in the utilization of nonfermentable carbon sources.
引文
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