Structural dynamics of the yeast Shwachman-Diamond syndrome protein (Sdo1) on the ribosome and its implication in the 60S subunit maturation

Protein & Cell

Meng-Qiu Dong¹  Dan Tan¹  Ningning Li²  Jianlin Lei²  Ning Gao²  Zhifei Li²  Kaige Yan²  Chengying Ma²  Yi Yuan²  Yixiao Zhang² 

[1] National Institute of Biological Sciences;School of Life Sciences, Tsinghua University;

关键词: ribosome biogenesis;    SBDS;    SDS;    Sdo1;    cryo-electron microscopy (cryo-EM);   

DOI  :  10.1007/s13238-015-0242-5

来源: DOAJ

【 摘 要 】

Abstract 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.

【 授权许可】

Unknown