| First Author | Yamagishi N | Year | 2003 |
| Journal | FEBS Lett | Volume | 555 |
| Issue | 2 | Pages | 390-6 |
| PubMed ID | 14644449 | Mgi Jnum | J:86751 |
| Mgi Id | MGI:2681405 | Doi | 10.1016/s0014-5793(03)01292-4 |
| Citation | Yamagishi N, et al. (2003) Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP. FEBS Lett 555(2):390-6 |
| abstractText | Hsp105alpha and Hsp105beta are mammalian members of the Hsp105/110 family, a diverged subgroup of the Hsp70 family. Here, we show that Hsp105alpha and Hsp105beta bind non-native protein through the beta-sheet domain and suppress the aggregation of heat-denatured protein in the presence of ADP rather than ATP. In contrast, Hsc70/Hsp40 suppressed the aggregation of heat-denatured protein in the presence of ATP rather than ADP. Furthermore, the overexpression of Hsp105alpha but not Hsp70 in COS-7 cells rescued the inactivation of luciferase caused by ATP depletion. Thus, Hsp105/110 family proteins are suggested to function as a substitute for Hsp70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress, in which the cellular ATP level decreases markedly. |
