AI Article Synopsis
- CarD is a crucial protein in Mycobacterium tuberculosis that helps regulate gene expression during its persistent infection state by interacting with RNA polymerase (RNAP) and downregulating certain genes.
- Researchers have determined the crystal structure of CarD bound to specific domains of the RNAP β-subunit, revealing important details about how this interaction supports the bacteria’s survival.
- The structure of CarD shows similarities to other RNAP-interacting proteins, but its C-terminal domain, necessary for its full function, has a unique DNA-binding configuration.
Article Abstract
CarD from Mycobacterium tuberculosis (Mtb) is an essential protein shown to be involved in stringent response through downregulation of rRNA and ribosomal protein genes. CarD interacts with the β-subunit of RNAP and this interaction is vital for Mtb's survival during the persistent infection state. We have determined the crystal structure of CarD in complex with the RNAP β-subunit β1 and β2 domains at 2.1 Å resolution. The structure reveals the molecular basis of CarD/RNAP interaction, providing a basis to further our understanding of RNAP regulation by CarD. The structural fold of the CarD N-terminal domain is conserved in RNAP interacting proteins such as TRCF-RID and CdnL, and displays similar interactions to the predicted homology model based on the TRCF/RNAP β1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3894638 | PMC |
| http://dx.doi.org/10.1016/j.str.2013.08.014 | DOI Listing |
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