Yet another job for the bacterial ribosome
Authors:Andrea Origi1,2, Ana Natriashivili1,2, Lara Knüpffer1, Clara Fehrenbach1, Kärt Denks1,2, Rosella Asti1 and Hans-Georg Koch1
doi: 10.15698/mic2019.11.698
Volume 6, pp. 524 to 526, published 17/10/2019.
1 Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs University Freiburg, 79104 Freiburg, Germany.
2 Faculty of Biology, Albert-Ludwigs University Freiburg, 79104 Freiburg, Germany.
Keywords:
SecA, signal recognition particle, SecYEG, protein targeting, uL23, ribosome.
Corresponding Author(s):
Conflict of interest statement:
The authors declare no conflict of interests.
Please cite this article as:
Andrea Origi, Ana Natriashivili, Lara Knüpffer, Clara Fehrenbach, Kärt Denks, Rosella Asti and Hans-Georg Koch (2019). Yet another job for the bacterial ribosome. Microbial Cell 6(11): 524-526. doi: 10.15698/mic2019.11.698
© 2019 Origi et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduc-tion in any medium, provided the original author and source are acknowledged.
Abstract:
The ribosome is a sophisticated cellular machine, composed of RNA and protein, which translates the mRNA-encoded genetic information into protein and thus acts at the center of gene expression. Still, the ribosome not only decodes the genetic information, it also coordinates many ribosome-associated processes like protein folding and targeting. The ribosomal protein uL23 is crucial for this coordination and is located at the ribosomal tunnel exit where it serves as binding platform for targeting factors, chaperones and modifying enzymes. This includes the signal recognition particle (SRP), which facilitates co-translational protein targeting in pro- and eukaryotes, the chaperone Trigger Factor and methionine aminopeptidase, which removes the start methionine in many bacterial proteins. A recent report revealed the intricate interaction of uL23 with yet another essential player in bacteria, the ATPase SecA, which is best known for its role during post-translational secretion of proteins across the bacterial SecYEG translocon.