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
AUTHORS (4)
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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