伴放线放线杆菌铁利用相关周质蛋白的特性分析
Characterization of a periplasmic protein involved in iron utilization of Actinobacillus actinomycetemcomitans.
作者信息
Willemsen P T, Vulto I, Boxem M, de Graaff J
机构信息
Department of Oral Microbiology, Academic Centre for Dentistry Amsterdam, The Netherlands.
出版信息
J Bacteriol. 1997 Aug;179(15):4949-52. doi: 10.1128/jb.179.15.4949-4952.1997.
Abstract
The periodontopathic bacterium Actinobacillus actinomycetemcomitans possesses a 35-kDa periplasmic iron-repressible protein. Its regulation is mediated by the Fur protein, as was inferred from the Fur-binding consensus sequence at the -35 position of the gene for the 35-kDa protein and from the relaxed expression of the gene in a mutant with an altered Fur-binding sequence. The 35-kDa protein, designated AfuA, has strong homology to HitA and FbpA of Haemophilus influenzae and Neisseria meningitidis, respectively, which serve as periplasmic iron transport proteins.
摘要
牙周病原菌伴放线放线杆菌拥有一种35 kDa的周质铁抑制蛋白。其调控由Fur蛋白介导，这是从该35 kDa蛋白基因-35位的Fur结合共有序列以及在Fur结合序列改变的突变体中该基因的松弛表达推断出来的。这种35 kDa的蛋白，命名为AfuA，分别与流感嗜血杆菌的HitA和脑膜炎奈瑟菌的FbpA有很强的同源性，它们作为周质铁转运蛋白。
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