Related Experiment Videos
A Zn(II)-translocating P-type ATPase from Proteus mirabilis
Summary
Researchers identified a Proteus mirabilis gene complementing an Escherichia coli mutant lacking the ZntA zinc transporter. This P. mirabilis gene encodes a zinc-translocating P-type ATPase, crucial for heavy metal transport.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- A Proteus mirabilis mutant defective in swarming was previously isolated.
- The mutation was mapped to a gene homologous to Escherichia coli zntA, which encodes a zinc-translocating P-type ATPase.
Purpose of the Study:
- To characterize the function of the P. mirabilis gene homologous to E. coli zntA.
- To confirm if the P. mirabilis gene encodes a functional zinc transporter.
Main Methods:
- Complementation of an E. coli zntA-disrupted mutant with the P. mirabilis gene.
- Assessing the P. mirabilis gene's ability to restore resistance to zinc and cadmium salts.
- Measuring ATP-driven 65Zn(II) uptake in everted membrane vesicles from E. coli strains.
Main Results:
- The P. mirabilis gene successfully complemented the zinc and cadmium sensitivity of the E. coli zntA mutant.
- Everted membrane vesicles from the zntA-disrupted E. coli strain showed a loss of ATP-driven 65Zn(II) uptake.
- Membrane vesicles from the complemented strain exhibited restored 65Zn(II) transport.
Conclusions:
- The P. mirabilis homologue of E. coli ZntA is a functional Zn(II)-translocating P-type ATPase.
- This P-type ATPase plays a role in heavy metal ion transport in P. mirabilis.