Figure 1 | Scientific Reports

Figure 1

From: Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns

Figure 1

hTRiC subunits can be chromatographically separated for downstream intact analysis. (a) Top and side views of the TRiC hexadecamer, showing subunit arrangement within the two antiparallel rings. Cycles of ATP hydrolysis catalyse ring opening and closure. (b) Reverse phase chromatogram of recombinant hTRiC, with peaks labelled by the predominant eluting subunit(s), as determined by Western blots shown in (c). (d) Intact, denatured mass spectra of reverse phase fractions containing each hTRiC subunit. For each assigned subunit mass, five peaks are annotated with triangles and one peak with its charge state. Fractions containing CCT5, CCT2, or CCT4 contain minor populations of masses corresponding to dimers, designated by two triangles annotated over five odd charge states. (Even charge states are not labelled with the double triangle notation for simplicity, but can be inferred to overlap with monomer peaks.) In the CCT2/CCT4 spectrum, CCT2 and CCT4 homodimers were detected as well as CCT2-CCT4 heterodimer.

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