The Zur-Regulated ZinT Protein Is an Auxiliary Component of the High-Affinity ZnuABC Zinc Transporter That Facilitates Metal Recruitment during Severe Zinc Shortage

Salmonella typhimurium 0303 health sciences Animal DNA-Binding Protein Bacterial Bacterial Protein Gene Expression Regulation, Bacterial; Mice; Acyl Carrier Protein; Bacterial Proteins; Animals; Salmonella typhimurium; DNA-Binding Proteins; Zinc 612 Gene Expression Regulation, Bacterial DNA-Binding Proteins Mice Zinc 03 medical and health sciences Gene Expression Regulation Bacterial Proteins Acyl Carrier Protein Animals Settore BIO/10 - BIOCHIMICA
DOI: 10.1128/jb.01310-09 Publication Date: 2010-01-23T03:03:24Z
ABSTRACT
ABSTRACT The pathways ensuring the efficient uptake of zinc are crucial for the ability of bacteria to multiply in the infected host. To better understand bacterial responses to zinc deficiency, we have investigated the role of the periplasmic protein ZinT in Salmonella enterica serovar Typhimurium. We have found that zinT expression is regulated by Zur and parallels that of ZnuA, the periplasmic component of the zinc transporter ZnuABC. Despite the fact that ZinT contributes to Salmonella growth in media containing little zinc, disruption of zinT does not significantly affect virulence in mice. The role of ZinT became clear using strains expressing a mutated form of ZnuA lacking a characteristic histidine-rich domain. In fact, Salmonella strains producing this modified form of ZnuA exhibited a ZinT-dependent capability to import zinc either in vitro or in infected mice, suggesting that ZinT and the histidine-rich region of ZnuA have redundant function. The hypothesis that ZinT and ZnuA cooperate in the process of zinc recruitment is supported by the observation that they form a stable binary complex in vitro . Although the presence of ZinT is not strictly required to ensure the functionality of the ZnuABC transporter, our data suggest that ZinT facilitates metal acquisition during severe zinc shortage.
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