Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis.
Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis.
复制标题
厌氧原生生物阴道毛滴虫的氢酶体铁氧还蛋白的分子分析。
DOI：
10.1073/pnas.87.16.6097
复制
发表时间：
1990
影响因子：
11.1
通讯作者：
Müller,M
中科院分区：
文献类型：
--
作者：
Johnson,PJ;d'Oliveira,CE;Gorrell,TE;Müller,M
我们测定了厌氧原生生物阴道毛滴虫[2Fe-2S]铁氧还蛋白的一级结构。这种蛋白质位于氢酶体中，由93个氨基酸组成。比较了T.迷走神经铁氧还蛋白与超过80种其他铁氧还蛋白显示出与需氧细菌恶臭假单胞菌的[2Fe-2S]恶臭铁氧还蛋白最接近的相似性，与脊椎动物的线粒体[2Fe-2S]铁氧还蛋白的相似性较小。这种相似性反映在整体的一级结构和半胱氨酸残基的间距协调的铁-硫中心。初级结构，但不是铁-硫中心的环境，也显示出与光合生物和盐细菌的[2Fe-2S]铁氧化还原蛋白的相似性。我们克隆并分析了T.迷走神经铁氧还蛋白基因该基因以单拷贝存在，并且没有内含子。它产生具有分别为16和18个核苷酸的异常短的5'和3'非翻译区的转录物。该基因的DNA序列分析预测在氨基末端另外8个氨基酸，其在纯化的蛋白质中不存在。该蛋白质的氨基末端区域的特征在于线粒体前序列的典型性质。
We have determined the primary structure of the [2Fe-2S]ferredoxin of the anaerobic protist Trichomonas vaginalis. This protein, situated in the hydrogenosome, is composed of 93 amino acids. A comparison of T. vaginalis ferredoxin with greater than 80 other ferredoxins shows the closest similarity to [2Fe-2S]putidaredoxin of the aerobic bacterium Pseudomonas putida and a lesser one to mitochondrial [2Fe-2S]ferredoxins of vertebrates. This similarity is reflected in the overall primary structure and in the spacing of cysteine residues coordinating the iron-sulfur center. The primary structure, but not the environment of the iron-sulfur center, also shows similarity with [2Fe-2S]ferredoxins of photosynthetic organisms and halobacteria. We have cloned and analyzed the T. vaginalis ferredoxin gene. The gene is present in a single copy and devoid of introns. It gives rise to a transcript with unusually short 5' and 3' untranslated regions of 16 and 18 nucleotides, respectively. DNA sequence analysis of the gene predicts an additional 8 amino acids at the amino terminus which are absent from the purified protein. This amino-terminal region of the protein is characterized by properties typical of mitochondrial presequences.