Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.3435.pdf
Reference111 articles.
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2. Zhang, S., Lockshin, C., Herbert, A., Winter, E. & Rich, A. Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae. EMBO J. 11, 3787–3796 (1992).
3. Boyer, A.S., Grgurevic, S., Cazaux, C. & Hoffmann, J.S. The human specialized DNA polymerases and non-B DNA: vital relationships to preserve genome integrity. J. Mol. Biol. 425, 4767–4781 (2013).
4. Yan, W. et al. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17, 4809–4817 (1998).This study revealed that the J-domain protein Zuo1 binds to ribosomes via ribosomal RNA and functions in concert with the Hsp70 Ssb.
5. Nelson, R.J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. & Craig, E.A. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71, 97–105 (1992).This work revealed that a large fraction of the Hsp70 Ssb is ribosome associated and involved in translation.
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