Structural highlights
Function
DNJC2_HUMAN Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.[1] [2] [3]
See Also
References
- ↑ Otto H, Conz C, Maier P, Wolfle T, Suzuki CK, Jeno P, Rucknagel P, Stahl J, Rospert S. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10064-9. Epub 2005 Jul 7. PMID:16002468 doi:http://dx.doi.org/10.1073/pnas.0504400102
- ↑ Hundley HA, Walter W, Bairstow S, Craig EA. Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science. 2005 May 13;308(5724):1032-4. Epub 2005 Mar 31. PMID:15802566 doi:http://dx.doi.org/10.1126/science.1109247
- ↑ Richly H, Rocha-Viegas L, Ribeiro JD, Demajo S, Gundem G, Lopez-Bigas N, Nakagawa T, Rospert S, Ito T, Di Croce L. Transcriptional activation of polycomb-repressed genes by ZRF1. Nature. 2010 Dec 23;468(7327):1124-8. doi: 10.1038/nature09574. PMID:21179169 doi:http://dx.doi.org/10.1038/nature09574
