ATP hydrolysis is essential for Bag-1M-mediated inhibition of the DNA binding by the glucocorticoid receptor

作者：Hong, Wei^*; Chen, Linfeng; Liu, Yunde; Gao, Weizhen

来源：Biochemical and Biophysical Research Communications, 2009, 390(1): 77-81.

DOI：10.1016/j.bbrc.2009.09.069

• ATP
• Bag-1
• Nuclear hormone receptor
• Chaperone
• Heat shock protein

The 70-kDa heat shock protein (Hsp70) is involved in providing the appropriate conformation of various nuclear hormone receptors, including the glucocorticoid receptor (GR). The Bcl-2 associated athanogene 1M (Bag-1M) is known to downregulate the DNA binding by the GR. Also, Bag-1M interacts with the ATPase domain of Hsp70 to modulate the release of the Substrate from Hsp70. In this study, we demonstrate that ATP hydrolysis enhances Bag-1M-n-tediated inhibition of the DNA binding by the GR. However, the inhibitory effect of Bag-1M was abolished when the intracellular ATP was depleted. In addition, a Bag-1M mutant lacking the interaction with Hsp70 did not influence the GR to bind DNA, suggesting the interaction of Bag-1M with Hsp70 in needed for its negative effect. These results indicate that ATP hydrolysis is essential for Bag-1M-mediated inhibition of the DNA binding by the GR and Hsp70 is a mediator for this process.

• 出版日期2009-12-4
• 单位天津医科大学