This gene encodes a member of the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described.[3]
Interactions
DNAJB6 has been shown to interact with Keratin 18.[4] It has been also shown that the aggregation of Aβ42 (a process involved in e.g. Alzheimer's disease) is retarded by DNAJB6 in a concentration-dependent manner, extending to very low sub-stoichiometric molar ratios of chaperone to peptide.[5]
References
↑Seki N, Hattori A, Hayashi A, Kozuma S, Miyajima N, Saito T (June 1999). "Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family". J Hum Genet. 44 (3): 185–9. doi:10.1007/s100380050139. PMID10319584.
↑Pei L (March 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". J Biol Chem. 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. PMID9915854.
↑Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M (2000). "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein". J. Biol. Chem. 275 (44): 34521–7. doi:10.1074/jbc.M003492200. PMID10954706.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Izawa I, Nishizawa M, Ohtakara K, et al. (2000). "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein". J. Biol. Chem. 275 (44): 34521–7. doi:10.1074/jbc.M003492200. PMID10954706.
Chuang JZ, Zhou H, Zhu M, et al. (2002). "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently". J. Biol. Chem. 277 (22): 19831–8. doi:10.1074/jbc.M109613200. PMID11896048.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. doi:10.1038/nature01782. PMID12853948.
Hanai R, Mashima K (2004). "Characterization of two isoforms of a human DnaJ homologue, HSJ2". Mol. Biol. Rep. 30 (3): 149–53. doi:10.1023/A:1024916223616. PMID12974469.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Liu Y, Zhu MC, Wang YJ, et al. (2004). "[Cloning of a DnaJ homolog chaperon PBP and its subcellular localization]". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 19 (6): 531–4. PMID15182641.
Berruti G, Martegani E (2005). "The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells". Biol. Reprod. 72 (1): 14–21. doi:10.1095/biolreprod.104.030866. PMID15342353.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.