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.
1. Hallstrom, T.C., Katzmann, D.J., Torres, R.J., Sharp, W.J. & Moye-Rowley, W.S. Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 18, 1147–1155 (1998).This work revealed, for the first time, that Ssz1 is an Hsp70 homolog that is involved in the activation of the transcription factor Pdr1.
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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