Structure of the Mtb CarD/RNAP -lobes complex reveals the molecular basis of interaction and presents a distinct DNA-binding domain for Mtb CarD. Academic Article uri icon


  • 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 -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 -subunit 1 and 2 domains at 2.1 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 1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold.

published proceedings

  • Structure

altmetric score

  • 3.35

author list (cited authors)

  • Gulten, G., & Sacchettini, J. C.

citation count

  • 28

complete list of authors

  • Gulten, Gulcin||Sacchettini, James C

publication date

  • October 2013