Disease relevance of bA16L21.2.1

• We show that HsDPH3 is the previously described human diphtheria toxin and Pseudomonas exotoxin A sensitivity required gene 1 and that DPH4 encodes a CSL zinc finger-containing DnaJ-like protein [1].
• The NMR structure of the N-terminal, DnaJ-like domain of murine polyomavirus tumor antigens (PyJ) has been determined to high precision, with root mean square deviations to the mean structure of 0.38 A for backbone atoms and 0.94 A for all heavy atoms of ordered residues 5-41 and 50-69 [2].
• Recent studies have shown that DnaJ-like family proteins can inhibit polyglutamine aggregation, a hallmark of many neurodegenerative diseases, including Huntington's disease (HD) [3].
• By using microarray and an invasion/metastasis lung cell line model, we identified the DnaJ-like heat shock protein 40, HLJ1, and found that the expression of HLJ1 correlates negatively with cancer cell invasion ability [4].
• Human neurone-specific DnaJ-like proteins, HSJ1a and HSJ1b, possess a J domain and a glycine/phenylalanine-rich region in common with E. coli DnaJ, although the overall amino acid identity is less than 23% [5].

High impact information on bA16L21.2.1

• DnaJ-like proteins function in association with Hsp70 molecular chaperones to facilitate protein folding [6].
• Domain requirements of DnaJ-like (Hsp40) molecular chaperones in the activation of a steroid hormone receptor [6].
• These results strongly suggest that HSJ1 proteins interfere with an endogenous DnaJ-like protein that is involved in uncoating [7].
• MsJ1, an alfalfa DnaJ-like gene, is tissue-specific and transcriptionally regulated during cell cycle [8].
• Although this type of DnaJ-like protein has not been found in other mammals, it may be essential for mammalian spermatogenesis [9].

Biological context of bA16L21.2.1

• These findings suggest that DnaJ-like proteins play an active role in regulating normal cellular events like protein degradation, morphogenesis and cell cycle progression [8].
• The predicted amino acid sequences of SGJ1 (47.5 kDa) and SGJ3 (46.6 kDa) exhibited about 70 to 91% homology to plant cytoplasmic DnaJ-like proteins [10].
• Protein motif analysis of nDnaJA1 sequence revealed motifs of DnaJ. nDnaJA1 was considered as type I DnaJ like the other members of DnaJA1 family [11].
• We have cloned a cDNA encoding a DnaJ-like protein from the human fibrosarcoma HT-1080 cDNA library [12].

Anatomical context of bA16L21.2.1

• Homologous components of this machinery have also been identified in other organelles such as the endoplasmic reticulum in which HSP70 and DnaJ-like homologs reside [13].

Associations of bA16L21.2.1 with chemical compounds

• Although most DnaJ-like proteins studied are ubiquitously expressed, some have restricted expression, so it is possible that some specific chaperones may affect polyglutamine aggregation in specific neurons [3].

Regulatory relationships of bA16L21.2.1

• DnaJ-like proteins are molecular chaperones that regulate Hsp70 ATPase activity both in protein folding, assembly and disassembly of protein complexes [8].

Other interactions of bA16L21.2.1

• Within the critical NPHP3/SLSN3 region we identified the gene KIAA0678 encoding a DnaJ-like protein [14].
• Candidate gene analysis of KIAA0678 encoding a DnaJ-like protein for adolescent nephronophthisis and Senior-Løken syndrome type 3 [14].

References