Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 2 of 2
Full-Text Articles in Life Sciences
Novel Small Rnas Expressed By Bartonella Bacilliformis Under Multiple Conditions Reveal Potential Mechanisms For Persistence In The Sand Fly Vector And Human Host, Shaun Wachter, Linda D. Hicks, Rahul Raghavan, Michael F. Minnick
Novel Small Rnas Expressed By Bartonella Bacilliformis Under Multiple Conditions Reveal Potential Mechanisms For Persistence In The Sand Fly Vector And Human Host, Shaun Wachter, Linda D. Hicks, Rahul Raghavan, Michael F. Minnick
Biology Faculty Publications and Presentations
Bartonella bacilliformis, the etiological agent of Carrión’s disease, is a Gram-negative, facultative intracellular alphaproteobacterium. Carrión’s disease is an emerging but neglected tropical illness endemic to Peru, Colombia, and Ecuador. B. bacilliformis is spread between humans through the bite of female phlebotomine sand flies. As a result, the pathogen encounters significant and repeated environmental shifts during its life cycle, including changes in pH and temperature. In most bacteria, small non-coding RNAs (sRNAs) serve as effectors that may post-transcriptionally regulate the stress response to such changes. However, sRNAs have not been characterized in B. bacilliformis, to date. We …
Direct Binding Of Tfeα Opens Dna Binding Cleft Of Rna Polymeras, Sung-Hoon Jun, Jaekyung Hyun, Hoyoung Kim, Michael S. Bartlett, Hyun-Soo Cho, Katsuhiko S. Murakami
Direct Binding Of Tfeα Opens Dna Binding Cleft Of Rna Polymeras, Sung-Hoon Jun, Jaekyung Hyun, Hoyoung Kim, Michael S. Bartlett, Hyun-Soo Cho, Katsuhiko S. Murakami
Biology Faculty Publications and Presentations
Opening of the DNA binding cleft of cellular RNA polymerase (RNAP) is necessary for transcription initiation but the underlying molecular mechanism is not known. Here, we report on the cryo-electron microscopy structures of the RNAP, RNAP-TFEα binary, and RNAPTFEα-promoter DNA ternary complexes from archaea, Thermococcus kodakarensis (Tko). The structures reveal that TFEα bridges the RNAP clamp and stalk domains to open the DNA binding cleft. Positioning of promoter DNA into the cleft closes it while maintaining the TFEα interactions with the RNAP mobile modules. The structures and photo-crosslinking results also suggest that the conserved aromatic residue in the extended winged-helix …