Fig. 4: The sperm-specific barrel is an RS-tethered TRiC chaperone.
From: Structural diversity of axonemes across mammalian motile cilia
a, TRiC is suspended between RS1 and RS2. b, TRiC contacts RS1 by small interfaces with RGS22 and AK8. c, TRiC is tethered to RS2 by a hitherto unidentified linker protein (grey) anchored to DNAJB13 and NME5. d, Assignment of subunit order in the barrel, based on the inherent asymmetries of TRiC, demonstrated by comparison with the structure of yeast TRiC33. Asterisk marks an unidentified luminal density of the distal ring (closer to RS2) in RS-tethered TRiC. This density binds at a location different from the binding site of the cochaperone Plp2 in yeast TRiC (grey density)33.
