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Srivastava, Devendra B.; Leon, Katherine; Osmundson, Joseph; Garner, Ashley L.; Weiss, Leslie A.; Westblade, Lars F.; Glickman, Michael S.; Landick, Robert; Darst, Seth A.; Stallings, Christina L.; Campbell, Elizabeth A.
Proceedings of the National Academy of Sciences - PNAS, 07/2013, Volume: 110, Issue: 31Journal Article
CarD, an essential transcription regulator in Mycobacterium tuberculosis , directly interacts with the RNA polymerase (RNAP). We used a combination of in vivo and in vitro approaches to establish that CarD is a global regulator that stimulates the formation of RNAP-holoenzyme open promoter (RPo) complexes. We determined the X-ray crystal structure of Thermus thermophilus CarD, allowing us to generate a structural model of the CarD/RPo complex. On the basis of our structural and functional analyses, we propose that CarD functions by forming protein/protein and protein/DNA interactions that bridge the RNAP to the promoter DNA. CarD appears poised to interact with a DNA structure uniquely presented by the RPo: the splayed minor groove at the double-stranded/single-stranded DNA junction at the upstream edge of the transcription bubble. Thus, CarD uses an unusual mechanism for regulating transcription, sensing the DNA conformation where transcription bubble formation initiates.
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