Paracoccidioides brasiliensis presents two different cDNAs encoding homologues of the fructose 1,6-biphosphate aldolase:: protein isolation, cloning of the cDNAs and genes, structural, phylogenetic, and expression analysis
Paracoccidioides brasiliensis presents two different cDNAs encoding homologues of the fructose 1,6-biphosphate aldolase:: protein isolation, cloning of the cDNAs and genes, structural, phylogenetic, and expression analysis
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DOI：
10.1016/j.fgb.2004.10.003
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发表时间：
2005-01-01
影响因子：
3
通讯作者：
Soares, CMD
中科院分区：
文献类型：
--
作者：
Carneiro, LC;de Faria, FP;Soares, CMD
蛋白质组学方法用于鉴定巴西副球孢子菌的39 kDa抗原。N-末端和内切蛋白酶Lys-C消化的肽的氨基酸序列显示该蛋白质是巴西假单胞菌的果糖1，6-二磷酸醛缩酶（FBA）II类。两个cDNA同源物，Pbfba 1和Pbfba 2，克隆和表征。pbfba 1编码一个预测的360个氨基酸的多肽，在一级结构上与真菌和细菌的相同酶高度同源。另一个DNA，Pbfba 2，编码一个多肽，预计是363个氨基酸。Pbfba 2的序列与Pbfba 1的序列差异显著。系统发育和分子生物学分析支持巴西对虾中FBA基因重复的概念，构成一个两成员家族。表达分析表明两种fbas基因在巴西对虾细胞中的差异表达。(C)2004爱思唯尔公司All rights reserved.
A proteomic approach was used to identify a 39 kDa antigen of Paracoccidioides brasiliensis. Amino acid sequences of the N-terminal and of endoproteinase Lys-C digested peptides revealed the protein to be a fructose 1,6-biphosphate aldolase (FBA) Class II of P. brasiliensis. Two cDNA homologues, Pbfba1 and Pbfba2, were cloned and characterized. Pbfba1 encoded a predicted polypeptide of 360 amino acids that was highly homologous in the primary structure to the same enzyme from fungi and bacteria. The other DNA, Pbfba2, encoded a polypeptide predicted to be 363 amino acids. The sequence of Pbfba2 differed significantly from Pbfba1. Phylogenetic and molecular analysis supports the concept of gene duplication for FBAs in P. brasiliensis, constituting a two-member family. Expression analysis demonstrated differential expression for both fbas genes in P. brasiliensis cells. (C) 2004 Elsevier Inc. All rights reserved.