Fig. 3: Negative charges of Tim17 transmembrane domains are crucial for presequence protein translocation. | Nature

Fig. 3: Negative charges of Tim17 transmembrane domains are crucial for presequence protein translocation.

From: Central role of Tim17 in mitochondrial presequence protein translocation

Fig. 3

a, ColabFold model of S. cerevisiae Tim17 (tan) and Tim23 (grey) heterodimer showing, as red sticks, the locations of negatively charged residues aspartic acid 17 (D17) and 76 (D76) and glutamic acid 126 (E126) within the transmembrane region of Tim17. b, Import of radiolabelled F1β (matrix), b2(167)Δ-DHFR (matrix) and b2(220)-DHFR (inner membrane-sorted) precursors into isolated mitochondria; subsequently, they were treated with proteinase K and subjected to SDS–PAGE and autoradiography. i*, intermediate. c, MTX preincubated radiolabelled b2(220)-DHFR was imported into isolated wild-type Tim17 or mutant mitochondria followed by BN–PAGE and autoradiography. TOM-b2(220)-DHFR, MPP and IMP processed b2(220)-DHFR was stabilized at the TOM complex.

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