REGULATION OF TRACE METAL UPTAKE IN BACTERIA

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 NikR是病原微生物的关键调控转录因子，这些病原微生物依赖镍酶，如尿素酶和NiFe-氢酶生存。如果没有适量的Ni2+，这些细菌就不能在某些条件下生存，例如低pH值或厌氧环境。然而，细胞内过量的Ni2+会导致细胞凋亡，因此调节细胞内Ni2+的浓度非常重要。出于这些原因，我们研究了细菌Ni2+调节转录因子NikR。到目前为止，我们已经发表了一些大肠杆菌NikR(EcNikR)的结构，这些结构有助于阐明NikR的总体结构、金属结合过程以及NikR与DNA结合的机制。这些结构包括：全长apo-EcNikR和Ni2+结合的调节域(Schreiter等人，自然结构生物学10(2003年)，794)，全长镍激活的EcNikR和EcNikR-操纵子DNA复合体(Schreiter等人，PNAS103(2006年)，13676)，以及EcNikR的apo，Cu2+和锌结合结构域(Phillips，等人，生物化学47(2008年)，1938年)。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. NikR is a key regulatory transcription factor for pathogenic microorganisms that depend on nickel enzymes such as urease and NiFe-hydrogenase for survival. Without a proper amount of Ni2+ these bacteria are unable to survive in certain conditions, such as low pH or anaerobic environments. However, an excess of Ni2+ in the cell can cause apoptosis, thus regulating the concentration of Ni2+ in the cell is of great importance. For these reasons we study the bacterial Ni2+-regulatory transcription factor, NikR. To date, we have published a number of structures of Escherichia coli NikR (EcNikR) that have helped elucidate the overall structure of NikR, the metal binding processes, and NikR-DNA binding mechanism. These structures include: the full-length apo-EcNikR and the Ni2+-bound regulatory domain (Schreiter et al., Nature Structural Biology 10 (2003), 794), full-length nickel-activated EcNikR and the EcNikR-operator DNA complex (Schreiter, et al., PNAS 103 (2006), 13676), and apo, Cu2+-, and Zn2+-bound metal binding domain (MBD) of EcNikR (Phillips, et al., Biochemistry 47 (2008), 1938).