ParB of Pseudomonas aeruginosa:: Interactions with its partner ParA and its target parS and specific effects on bacterial growth
ParB of Pseudomonas aeruginosa:: Interactions with its partner ParA and its target parS and specific effects on bacterial growth
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DOI：
10.1128/jb.186.20.6983-6998.2004
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发表时间：
2004-10-01
影响因子：
3.2
通讯作者：
Jagura-Burdzy, G
中科院分区：
文献类型：
--
作者：
Bartosik, AA;Lasocki, K;Jagura-Burdzy, G
研究了铜绿假单胞菌的par基因，以增加对其在细菌细胞中的作用机制和作用的理解。ParB蛋白的关键特性已被鉴定，并与蛋白质的不同部分相关。ParB-ParB相互作用结构域在体内和体外定位于C-末端56个氨基酸（aa）; C末端的7个aa起重要作用。铜绿假单胞菌ParB的二聚化结构域可与来自质粒RK 2（IncP 1组）的科尔布的二聚化结构域互换。ParB的C-末端部分也参与ParB-ParA相互作用。纯化的ParB特异性结合到含有假定的parS序列的DNA上，该序列基于枯草芽孢杆菌、恶臭假单胞菌和天蓝色链霉菌染色体中发现的共有序列。ParB的过量产生显示出抑制位于parS附近的基因的功能。这种“沉默”依赖于parS序列及其方向。铜绿假单胞菌ParB或其N-末端部分的过量产生也导致铜绿假单胞菌和恶臭假单胞菌而不是大肠杆菌细胞生长的抑制。由于该抑制性决定簇的位置远离二聚化或与帕拉对应物相互作用所需的ParB片段，因此该结果可能表明铜绿假单胞菌ParB的N末端在与宿主细胞组分相互作用中的作用。
The par genes of Pseudomonas aeruginosa have been studied to increase the understanding of their mechanism of action and role in the bacterial cell. Key properties of the ParB protein have been identified and are associated with different parts of the protein. The ParB- ParB interaction domain was mapped in vivo and in vitro to the C-terminal 56 amino acids (aa); 7 aa at the C terminus play an important role. The dimerization domain of P. aeruginosa ParB is interchangeable with the dimerization domain of KorB from plasmid RK2 (IncP1 group). The C-terminal part of ParB is also involved in ParB-ParA interactions. Purified ParB binds specifically to DNA containing a putative parS sequence based on the consensus sequence found in the chromosomes of Bacillus subtilis, Pseudomonas putida, and Streptomyces coelicolor. The overproduction of ParB was shown to inhibit the function of genes placed near parS. This "silencing" was dependent on the parS sequence and its orientation. The overproduction of P. aeruginosa ParB or its N-terminal part also causes inhibition of the growth of P. aeruginosa and P. putida but not Escherichia coli cells. Since this inhibitory determinant is located well away from ParB segments required for dimerization or interaction with the ParA counterpart, this result may suggest a role for the N terminus of P. aeruginosa ParB in interactions with host cell components.