Activities of the cochaperones Hap46/BAG-1M and Hap50/BAG-1L and isoforms.
Since their discovery about a decade ago, human Hap46/BAG-1M, the larger isoform Hap50/BAG-1L, and related structures have caused quite some astonishment because of the seemingly unlimited array of possible interaction partners belonging to completely unrelated protein families. This problem was partially resolved when it was realized that molecular chaperones of the heat shock protein family Hsp70 are major primary association partners, which in turn, are able to bind a wide variety of unrelated protein structures, thus forming ternary complexes. Moreover, the protein folding activity of Hsp70 chaperones is affected; hence, the designation "cochaperones." Although many different proteins require mediation by Hsp70 chaperones for interactions with Hap50/BAG-1L, Hap46/BAG-1M, and isoforms, several other partner proteins are able to associate directly. In addition, Hap46/BAG-1M and Hap50/BAG-1L are also able to interact with DNA by making use of a positively charged region close to the amino terminal end of the polypeptide chain. This is the molecular basis for their effects on transcriptional activities, which are emphasized in this review and for which a molecular model is presented.
Gehring
Ulrich
U
Universität Heidelberg, Percent Molekulare Evolution and Genomik, Im Neuenheimer Feld 230, D-69120 Heidelberg. RU-Gehring@T-online.de
D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008957:Models, Genetic; D018832:Molecular Chaperones / Q000378:metabolism*; D011485:Protein Binding; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D014158:Transcription, Genetic
C091732:BCL2-associated athanogene 1 protein; D004268:DNA-Binding Proteins; D018832:Molecular Chaperones; D020033:Protein Isoforms; D014157:Transcription Factors; D004247:DNA