AI Article Synopsis
- The alpha-proteobacterium Wolbachia pipientis influences its host's reproductive biology to ensure its own transmission, but studying it has been challenging due to its strict growth requirements and limited genetic tools.
- Researchers have determined the structure of Wolbachia's alpha-DsbA1 protein, which is crucial for the oxidative folding of proteins and demonstrates the highest reducing potential among characterized DsbA enzymes.
- Unlike its E. coli counterpart, Wolbachia's alpha-DsbA1 has distinct surface traits and a specialized function, laying the groundwork for future chemical genetics experiments.
Article Abstract
The alpha-proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host's reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the lack of genetic transformation have hampered analysis of the molecular basis of these manipulations. Structure determination of key Wolbachia proteins will enable the development of inhibitors for chemical genetics studies. Wolbachia encodes a homologue (alpha-DsbA1) of the Escherichia coli dithiol oxidase enzyme EcDsbA, essential for the oxidative folding of many exported proteins. We found that the active-site cysteine pair of Wolbachia alpha-DsbA1 has the most reducing redox potential of any characterized DsbA. In addition, Wolbachia alpha-DsbA1 possesses a second disulfide that is highly conserved in alpha-proteobacterial DsbAs but not in other DsbAs. The alpha-DsbA1 structure lacks the characteristic hydrophobic features of EcDsbA, and the protein neither complements EcDsbA deletion mutants in E. coli nor interacts with EcDsbB, the redox partner of EcDsbA. The surface characteristics and redox profile of alpha-DsbA1 indicate that it probably plays a specialized oxidative folding role with a narrow substrate specificity. This first report of a Wolbachia protein structure provides the basis for future chemical genetics studies.
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| http://dx.doi.org/10.1089/ars.2008.2420 | DOI Listing |
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