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Glen Borchert

The goal of my postdoctoral research is to explore potential roles for the Signal Recognition Particle 9/14 (SRP9/14) complex proteins in primate cells, where they are intriguingly expressed over 20-fold higher than the other protein components of the larger signal recognition particle (SRP). All secreted and membrane-destined proteins encode a leader or signal peptide that constitutes the first part of the nascent protein to exit the ribosome. Signal peptide recognition by the SRP signal domain causes the SRP RNA to bend 90° and insert its Alu Domain (bound by SRP9 and SRP14) into the ribosome where, through making tRNA-like contacts, it halts translation by preventing the association of any further tRNAs. Since cytoplasmic SRP9/14 (in complex with small cytoplasmic Alu RNAs) exists free from the full Signal Recognition Particle, I am exploring mechanisms by which scAlus bound by SRP9 and SRP14 could potentially halt translation of human 3' UTRs containing Alu repeat sequences.

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