Journal: Communications Biology

Article Title: A small molecule allosterically activates SecA dependent secretion

doi: 10.1038/s42003-026-09623-w

Figure Lengend Snippet: A–B MANT-ADP (1 µM; black trace) binds to the wild-type translocase ( A ; grey trace; 0.4 µM SecA 2 ; 1 µM SecYEG-IMVs) or to the wild-type SecA 2 ( B ; grey trace), at 25 o C, increases its fluorescence intensity and then remains relatively stable. The black arrow indicates time of translocase ( A ) or SecA 2 ( B ) addition. Subsequent addition of 1 µM MANT-ADP buffer (50 µl; red arrow) containing preprotein (10 µM; purple trace), or HSI#6 (10 µM; orange trace), caused an immediate drop in the fluorescence intensity, while addition of only buffer (grey trace), or buffer with DMSO (yellow trace), did not have that effect. All samples, except the grey trace-sample (buffer), contain the same final DMSO concentration. n = 3. Repeats were normalized (to 0% = MANT-ADP intensity; 100% = MANT-ADP plus partner intensity) and averaged. The effect of higher HSI#6 concentrations is shown in Supplementary Fig. .

Article Snippet: The fluorescence intensity of 1 μM MANT-ADP increased upon addition of the holoenzyme (Fig. , black arrow; 0.4 μM SecA 2, 1 μM SecYEG-IMVs preincubated for 2 min, ice) and remained stable (grey trace), indicating tight ADP binding , .

Techniques: Fluorescence, Concentration Assay