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Published August 2014 | Accepted Version
Journal Article Open

Co-translational protein targeting to the bacterial membrane


Co-translational protein targeting by the Signal Recognition Particle (SRP) is an essential cellular pathway that couples the synthesis of nascent proteins to their proper cellular localization. The bacterial SRP, which contains the minimal ribonucleoprotein core of this universally conserved targeting machine, has served as a paradigm for understanding the molecular basis of protein localization in all cells. In this review, we highlight recent biochemical and structural insights into the molecular mechanisms by which fundamental challenges faced by protein targeting machineries are met in the SRP pathway. Collectively, these studies elucidate how an essential SRP RNA and two regulatory GTPases in the SRP and SRP receptor (SR) enable this targeting machinery to recognize, sense and respond to its biological effectors, i.e. the cargo protein, the target membrane and the translocation machinery, thus driving efficient and faithful co-translational protein targeting. This article is part of a Special Issue entitled: Protein trafficking & Secretion.

Additional Information

© 2013 Elsevier B.V. Received 10 August 2013; Received in revised form 9 October 2013; Accepted 16 October 2013; Available online 24 October 2013. We thank Sandra Schmid, Jennifer Doudna, Peter Walter, Ramanujan Hegde, Douglas Rees, Raymond Deshaies and Bil Clemons for support and insightful discussions over the years, and David Akopian for critical reading of the manuscript. S.S. was supported by NIH grant GM078024 and by career awards from the Henry and Camille Dreyfus foundation, the Arnold and Mabel Beckman foundation, and the David and Lucile Packard foundation. I.S. was supported by a grant from the Betty and Gordon Moore Foundation.

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Accepted Version - nihms534497.pdf


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