伯氏疏螺旋体 cp32 BpaB 调节噬菌体 NucP 核酸内切酶和 SsbP 单链 DNA 结合蛋白的表达。
Borrelia burgdorferi cp32 BpaB modulates expression of the prophage NucP nuclease and SsbP single-stranded DNA-binding protein.
机构信息
Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, Kentucky, USA.
出版信息
J Bacteriol. 2012 Sep;194(17):4570-8. doi: 10.1128/JB.00661-12. Epub 2012 Jun 22.
Abstract
The Borrelia burgdorferi BpaB proteins of the spirochete's ubiquitous cp32 prophages are DNA-binding proteins, required both for maintenance of the bacteriophage episomes and for transcriptional regulation of the cp32 erp operons. Through use of DNase I footprinting, we demonstrate that BpaB binds the erp operator initially at the sequence 5'-TTATA-3'. Electrophoretic mobility shift assays indicated that BpaB also binds with high affinity to sites located in the 5' noncoding regions of two additional cp32 genes. Characterization of the proteins encoded by those genes indicated that they are a single-stranded DNA-binding protein and a nuclease, which we named SsbP and NucP, respectively. Chromatin immunoprecipitation indicated that BpaB binds erp, ssbP, and nucP in live B. burgdorferi. A mutant bacterium that overexpressed BpaB produced significantly higher levels of ssbP and nucP transcript than did the wild-type parent.
摘要
螺旋体普遍存在的 cp32 原噬菌体的博莱霉素 burgdorferi BpaB 蛋白是 DNA 结合蛋白，对于维持噬菌体外体和 cp32 erp 操纵子的转录调控都是必需的。通过使用 DNase I 足迹法，我们证明 BpaB 最初在序列 5'-TTATA-3'处结合 erp 操纵子。电泳迁移率变动分析表明，BpaB 还与另外两个 cp32 基因的 5'非编码区中的高亲和力结合位点结合。那些基因所编码的蛋白质的特性表明它们是单链 DNA 结合蛋白和核酸酶，我们分别将它们命名为 SsbP 和 NucP。染色质免疫沉淀表明，BpaB 在活的 B. burgdorferi 中结合 erp、ssbP 和 nucP。与野生型亲本相比，过表达 BpaB 的突变细菌产生的 ssbP 和 nucP 转录本水平显著更高。
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