The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.
The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.
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DOI：
10.1093/nar/gkac292
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发表时间：
2022-05-20
影响因子：
14.9
通讯作者：
Wong, Kam-Bo
中科院分区：
文献类型：
--
作者：
Yang, Lei;Lee, Ka-Ming;Yu, Conny Wing-Heng;Imai, Hirotatsu;Choi, Andrew Kwok-Ho;Banfield, David K.;Ito, Kosuke;Uchiumi, Toshio;Wong, Kam-Bo
真核uL 11在N-末端含有一个保守的MPPKFDP基序，这在古细菌和细菌同源物中没有发现。在这里，我们确定了解决方案的结构的人uL 11的NMR光谱和表征其骨干动力学的15 N-1H弛豫实验。我们发现，这些N-末端残基是非结构化的和灵活的。与核糖体结合的uL 11的结构比较表明，人uL 11的N-末端结构域和C-末端结构域之间的接头区域本质上是无序的，并且只有当与核糖体结合时才变得结构化。突变研究表明，N-末端保守的MPPKFDP基序参与与P-复合物及其延伸的突起结构域的uL 10在体外的相互作用。在杂合核糖体和酵母诱变研究中，MPPKFDP基序的截短也减少了聚苯丙氨酸的合成。此外，在酵母核糖体中，螺旋-1的保守GPLG基序的G→A/P取代使聚苯丙氨酸合成减少到9-32%。我们提出，uL 11的灵活的N-末端残基，它可以从uL 11的N-末端结构域延伸到250 bp，可以与uL 10形成短暂的相互作用，帮助获取和固定到一个位置，准备招募传入的翻译因子，促进蛋白质合成。
Eukaryotic uL11 contains a conserved MPPKFDP motif at the N-terminus that is not found in archaeal and bacterial homologs. Here, we determined the solution structure of human uL11 by NMR spectroscopy and characterized its backbone dynamics by 15N–1H relaxation experiments. We showed that these N-terminal residues are unstructured and flexible. Structural comparison with ribosome-bound uL11 suggests that the linker region between the N-terminal domain and C-terminal domain of human uL11 is intrinsically disordered and only becomes structured when bound to the ribosomes. Mutagenesis studies show that the N-terminal conserved MPPKFDP motif is involved in interacting with the P-complex and its extended protuberant domain of uL10 in vitro. Truncation of the MPPKFDP motif also reduced the poly-phenylalanine synthesis in both hybrid ribosome and yeast mutagenesis studies. In addition, G→A/P substitutions to the conserved GPLG motif of helix-1 reduced poly-phenylalanine synthesis to 9–32% in yeast ribosomes. We propose that the flexible N-terminal residues of uL11, which could extend up to ∼25 Å from the N-terminal domain of uL11, can form transient interactions with the uL10 that help to fetch and fix it into a position ready for recruiting the incoming translation factors and facilitate protein synthesis.
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影响因子：
5.5
作者：
Hess, Berk
通讯作者：
Hess, Berk
通过化学移动扰动和诱变分析，滴虫，核糖体灭活蛋白与核糖体茎蛋白P2之间的相互作用。
影响因子：
14.9
作者：
Chan, Denise S B;Chu, Lai-On;Lee, Ka-Ming;Too, Priscilla H M;Ma, Kit-Wan;Sze, Kong-Hung;Zhu, Guang;Shaw, Pang-Chui;Wong, Kam-Bo
通讯作者：
Wong, Kam-Bo
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL
影响因子：
2.7
作者：
DELAGLIO, F;GRZESIEK, S;BAX, A
通讯作者：
BAX, A
影响因子：
8.8
作者：
Flis, Julia;Holm, Mikael;Budkevich, Tatyana V.
通讯作者：
Budkevich, Tatyana V.