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伯氏疏螺旋体中的寡肽通透酶:由染色体和质粒位点编码的假定肽结合成分。

Oligopeptide permease in Borrelia burgdorferi: putative peptide-binding components encoded by both chromosomal and plasmid loci.

作者信息

Bono James L, Tilly Kit, Stevenson Brian, Hogan Dan, Rosa Patricia

机构信息

Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, 903 South Fourth Street, Hamilton, MT 59840, USA.

出版信息

Microbiology (Reading). 1998 Apr;144 ( Pt 4):1033-1044. doi: 10.1099/00221287-144-4-1033.

Abstract

To elucidate the importance of oligopeptide permease for Borrelia burgdorferi, the agent of Lyme disease, a chromosomal locus in B. burgdorferi that encodes homologues of all five subunits of oligopeptide permease has been identified and characterized. B. burgdorferi has multiple copies of the gene encoding the peptide-binding component, OppA; three reside at the chromosomal locus and two are on plasmids. Northern analyses indicate that each oppA gene is independently transcribed, although the three chromosomal oppA genes are also expressed as bi- and tri-cistronic messages. Induction of one of the plasmid-encoded oppA genes was observed following an increase in temperature, which appears to be an important cue for adaptive responses in vivo. The deduced amino acid sequences suggest that all five borrelial oppA homologues are lipoproteins, but the protease-resistance of at least one of them in intact bacteria is inconsistent with outer-surface localization. Insertional inactivation of a plasmid-encoded oppA gene demonstrates that it is not essential for growth in culture.

摘要

为阐明寡肽通透酶对莱姆病病原体伯氏疏螺旋体的重要性,已鉴定并表征了伯氏疏螺旋体中一个编码寡肽通透酶所有五个亚基同源物的染色体位点。伯氏疏螺旋体具有编码肽结合成分OppA的基因的多个拷贝;三个位于染色体位点,两个位于质粒上。Northern分析表明,每个oppA基因都是独立转录的,尽管三个染色体oppA基因也作为双顺反子和三顺反子信息表达。在温度升高后观察到其中一个质粒编码的oppA基因的诱导,这似乎是体内适应性反应的一个重要线索。推导的氨基酸序列表明,所有五个伯氏疏螺旋体oppA同源物都是脂蛋白,但其中至少一个在完整细菌中的蛋白酶抗性与外表面定位不一致。质粒编码的oppA基因的插入失活表明它对培养中的生长不是必需的。

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