Fig. 1.

Hsp40 and Hsp70 interact with a region of the NTD containing the FQNLF motif. a Domain organization of the androgen receptor with an indication, in gray, of the regions of sequence of the transactivation domain (NTD) that are partially folded, of the structures of the globular domains (DBD and LBD) and of the two constructs used in this work (NTD_1-155 and NTD_144-450)^26,29. b Changes in the intensity of the resonances of 33 μM NTD_1-155 caused by 0.5 (orange for Hsp40, red for Hsp70) and 1 (blue for Hsp40, green for Hsp70) molar equivalents of Hsp40 (top) and Hsp70 (bottom), in the absence of added nucleotides, with an indication of the accessible area buried upon folding (AABUF)⁴², of the disorder propensity as predicted by PONDR⁶⁹, and of the interaction motif identified in this work, where positively charged residues are shown in blue, hydrophobic residues are shown in green and the residues labeled with a black dot are shown in c. c Selected regions of the ¹H,¹⁵N-HSQC spectrum of 33 μM NTD_1-155 in the presence of 0.5 and 1 molar equivalents of Hsp40 (top) and Hsp70 (bottom), in the absence of added nucleotides, that illustrate that no chemical shift changes are observed upon interaction with Hsp40 and Hsp70. In c only the contour of lowest intensity is shown for clarity, colored according to the code used in b