DnaJ

Gamer, J., Bujard, H., Bukua, B. (1992). Physical interaction between heat shock proteins DnaK, DnaJ, CJtpE the bacterial heat shock transcription factor sigma 32. Cell 69, 833-842. 

Langer, T., Lu., C, Echols, H., Flanagan, J, Hayer, M.K., Hartl, F.-U. (1992). Successive action of Dnak, DnaJ, GroEL along the pathway of chaperone mediated protein folding. Nature 356, 683-689. 

Silver, P.A. Way, J.C. (1993). Eukaryotic DnaJ homologs and the specificity of hsp70 activity. Cell 74, 5-6. 

Table 36-3. Some major features of the structure and function of human mitochondrial DNAJ...

DnaJ DnaJ molecular chaperone homology domain E(MFP)AB 21(21) 36(36) 1BQ0... 

Dittmar KD, Banach M, Galigniana MD, Pratt WB. (1998) The role of DNAJ-Kke proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60. hsp70 foldosome complex. J Biol Chem. 273, 7358-7366. 

Gautschi M, Lilie H, Ftinfschilling U, Mun A, Ross S, Lithgow T, Riicknagel P, Rospert S (2001) RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Sszlp and zuotin. Proc Natl Acad Sci USA 98 3762-3767... 

Yan W, Schilke B, Pfund C, Walter W, Kim S, Craig EA (1998) Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J 17 4809-4817... 

Szabo A, Langer T, Schroder H, Flanagan J, Bukau B, Harti FU (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci USA 91 10345-10349... 

FIGURE 4-30 Chaperones in protein folding. The cyclic pathway by which chaperones bind and release polypeptides is illustrated for the . coli chaperone proteins DnaK and DnaJ, homologs of the eukaryotic chaperones Hsp70 and Hsp40. The chaperones do not actively promote the folding of the substrate protein, but instead prevent aggregation of unfolded peptides. For a population of polypeptides, some... 

Many of the chaperones double as heat shock-proteins (Hsp). When a cell is put under stress that can cause proteins to denature, such as too high a temperature, it produces heat-shock proteins. Their names are abbreviated to Hsp plus their subunit molecular mass in kDa. Hsp70, for example, is a ubiquitous heat-shock protein in eukaryotes. It is known in E. coli as DnaK for historical reasons because it was first discovered from a supposed role in DNA replication. Hsp70 is also important in protein trafficking and the conveying of proteins across membranes, because the denatured state is important in these processes. In protein biosynthesis, the unfolded state of the nascent polypeptide chain is passed on to DnaK, which maintains it in an extended form. The chain, under the influence of ATP and co-chaperones such as DnaJ and GrpE, is handed over to GroEL. 

Fig. 2. Kinetic curves of the products formation from CNA. b-DPOAi + - DNAj o - CPDAj Catalyst N°9j isopropanol-water (90 10), 100 cm3j CNA 5 gj CNA/catalyst 0 P 1 bar T G0°Cj stirred tank reactor.

Izawa, I., Nishizawa, M., Ohtakara, K, Ohtsuka, K, Inada, H., and Inagaki, M. (2000). Identification of Mij, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein./. Biol. Chem. 275, 34521-34527. 

Schweitzer, B.A. and Kool, E.T. (1995) Hydrophobic, non-hydrogen-bonding bases and base pairs in DNAJ. Am. Chem.Soc., 117, 1863-1872. 

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