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Identification Of Protein UbiD And UbiG Engaged In Ubiquinone Biosynthesis From Chlamydophila Pneumoniae AR39

Posted on:2007-12-08Degree:DoctorType:Dissertation
Country:ChinaCandidate:J LiuFull Text:PDF
GTID:1104360185497254Subject:Biochemistry and Molecular Biology
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Chlamydophilia were strictly parasite prokaryocytes in eukaryocytes, which had compact relation with Gram-negative bacterium. Microbiologically, Chlamydophilia were characterized by a developmental cycle involving metabolically inactive infectious developmental form called the elementary body (EB). After entry into the target host cell, EB differentiated into a metabolically active developmental form called the reticular body (RB). In twenty hours after infection, RB can produce many elementary bodies through division. Mature EBs were diffused through host lysis and began a new round of life cycle. Chlamydophila pneumoniae cause acute or chronic non-typical pneumoniae through their infection on epithetical cells of human respiratory system. Some researches show that Chlamydophila pneumoniae also can arouse atherogenesis or other diseases in cardiovascular system.Because their specific life cycles, chlamydial biochemistry and molecular biology were poorly understood. Many researches mainly focused on the diagnosis and treatment of diseases caused by Chlamydophila pneumonia. The genome of Chlamydophila pneumoniae AR39 was sequenced in 2000 and report showed that about 531 proteins in genomic encoding 1128 proteins were described as hypothetical proteins, which possess 47.1 percent in all encoding proteins. So identification functions of hypothetical proteins in Chlamydophila pneumoniae will benefit for clear apprehension of life cycle and relative pathogenic mechanisms. According to genomic analysis, synthases, hydroxylases, decarboxylases and methylases engaged in synthesis and metabolism of aromatic...
Keywords/Search Tags:Chlamydophila pneumoniae, UbiD, UbiG, ubiquinone, succinate, 4-hydroxybenzoic acid, decarboxylase, homologous recombination
PDF Full Text Request
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