Human EIF6 (Eukaryotic Translation Initiation Factor 6) ELISA Kit

The human Shwachman-Diamond syndrome (SDS) is an autosomal recessive disease caused by mutations in a highly conserved ribosome assembly factor SBDS. The functional role of SBDS is to cooperate with another assembly factor, elongation factor 1-like (Efl1), to promote the release of eukaryotic initiation factor 6 (eIF6) from the late-stage cytoplasmic 60S precursors. In the present work, we characterized, both biochemically and structurally, the interaction between the 60S subunit and SBDS protein (Sdo1p) from yeast. Our data show that Sdo1p interacts tightly with the mature 60S subunit in vitro through its domain I and II, and is capable of bridging two 60S subunits to form a stable 2:2 dimer. Structural analysis indicates that Sdo1p bind to the ribosomal P-site, in the proximity of uL16 and uL5, and with direct contact to H69 and H38. The dynamic nature of Sdo1p on the 60S subunit, together with its strategic binding position, suggests a surveillance role of Sdo1p in monitoring the conformational maturation of the ribosomal P-site. Altogether, our data support a conformational signal-relay cascade during late-stage 60S maturation, involving uL16, Sdo1p, and Efl1p, which interrogates the functional P-site to control the departure of the anti-association factor eIF6.

The protein p27(BBP)supercript stop (alias eIF6) occurs in yeast and mammalian epithelial cells. It is essential for ribosome genesis and has also been implicated in the functionality of integrins and intermediate filaments. By immunoblot, we show that homogenized integument from Sepia officinalis (Cephalopoda, Mollusca) contains a protein with immunological properties that closely resemble those of p27(BBP). We also demonstrate, by immunogold electron microscopy with an indirect immunoreaction technique on ultrathin sections of human skin and Sepia integument, that p27(BBP) is constantly present in both species in epithelial cells, fibroblasts, and muscle fibers. It is found in the vicinity of intermediate filaments, in nucleoli, along the internal wall of the nuclear membrane, and in association with desmosomes and hemidesmosomes and occasionally occurs extracellularly. Thus, the structure and function of p27(BBP) seem to have been highly conserved throughout evolution; the protein appears to be essential in eukaryotic cells in which it interacts with several ultrastructural components of diverse function.