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

doi:10.1007/s13238-015-0242-5

Protein & Cell

2016, Vol. 07

Issue (03): 187-200 https://doi.org/10.1007/s13238-015-0242-5

本期目录

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

Chengying Ma¹,Kaige Yan¹,Dan Tan^2,³,Ningning Li¹,Yixiao Zhang¹,Yi Yuan¹,Zhifei Li¹,Meng-Qiu Dong^2,³,Jianlin Lei¹,Ning Gao^1,^*(

)

1. School of Life Sciences, Tsinghua University, Beijing 100084, China
2. National Institute of Biological Sciences, Beijing 102206, China
3. Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, China

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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.

Key words： ribosome biogenesis SBDS SDS Sdo1 cryo-electron microscopy (cryo-EM)

收稿日期: 2015-12-04 出版日期: 2016-04-13

Corresponding Author(s): Ning Gao

引用本文:

. [J]. Protein & Cell, 2016, 07(03): 187-200.
Chengying Ma,Kaige Yan,Dan Tan,Ningning Li,Yixiao Zhang,Yi Yuan,Zhifei Li,Meng-Qiu Dong,Jianlin Lei,Ning Gao. Structural dynamics of the yeast Shwachman-Diamond syndrome protein (Sdo1) on the ribosome and its implication in the 60S subunit maturation. Protein Cell, 2016, 07(03): 187-200.

链接本文:

https://academic.hep.com.cn/pac/CN/10.1007/s13238-015-0242-5
https://academic.hep.com.cn/pac/CN/Y2016/V07/I03/187

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