Human endogenous retroviruses (HERV) are inherited sequences of our genome that closely resemble HIV. The expression of these sequences through the production of genomic RNA and proteins has been linked to various cancers, autoimmune diseases and neurodegenerative disorders. Of particular interest is HERV-K, a relatively recent insertion to our genome that is the most biologically active HERV. Expression of viral proteins is dependent on a 433-nucleotide long region on the HERV-K genome, the Rec response element (RcRE), which interacts specifically with the viral protein Rec and the resulting ribonucleoprotein complex recruits the cellular nuclear export machinery. The RcRE is homologous to the better studied HIV Rev response element (RRE). Using small-angle X-ray scattering (SAXS), we have solved the 3-D structure of the RcRE. The overall shape resembles the unique topology of the HIV RRE. Thus, the three-dimensional structure is conserved, despite low sequence similarity. The structural conservation explains why the HIV Rev protein is able to interact with both the HIV RRE and the HERV-K RcRE. Although SAXS has the advantage of studying a molecule in solution, it is limited in resolution and does not allow for the designation of individual stem loops. In order to identify individual domains, modifications were introduced by PCR mutagenesis, followed by in vitro transcription of linearized DNA. The resulting RNA was resolved on a non-denaturing gel with the desired band excised in order to purify. The RNA was then eluted from the gel via passive diffusion and concentrated on spin columns. The purified RNA was analyzed by SAXS at the Argonne National Laboratory. The resulting images will serve to further elucidate the 3-D structure of HERV-K RcRE.

Solution conformation of the HERV-K nuclear export element

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.