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• W2912058239 startingPage "33" @default.
• W2912058239 abstract "Disulphide bonds are widely used among all domains of life to provide structural stability to proteins and to regulate enzyme activity. Chlamydia spp. are obligate intracellular bacteria that are especially dependent on the formation and degradation of protein disulphide bonds. Members of the genus Chlamydia have a unique biphasic developmental cycle alternating between two distinct cell types; the extracellular infectious elementary body (EB) and the intracellular replicating reticulate body. The proteins in the envelope of the EB are heavily cross-linked with disulphides and this is known to be critical for this infectious phase. In this review, we provide a comprehensive summary of what is known about the redox state of chlamydial envelope proteins throughout the developmental cycle. We focus especially on the factors responsible for degradation and formation of disulphide bonds in Chlamydia and how this system compares with redox regulation in other organisms. Focussing on the unique biology of Chlamydia enables us to provide important insights into how specialized suites of disulphide bond (Dsb) proteins cater for specific bacterial environments and lifecycles." @default.
• W2912058239 created "2019-02-21" @default.
• W2912058239 creator A5011456426 @default.
• W2912058239 creator A5040201335 @default.
• W2912058239 creator A5067036789 @default.
• W2912058239 creator A5077570627 @default.
• W2912058239 date "2019-01-02" @default.
• W2912058239 modified "2023-10-17" @default.
• W2912058239 title "Life inside and out: making and breaking protein disulfide bonds in<i>Chlamydia</i>" @default.
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