Solution structure of human P1•P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome.
Solution structure of human P1•P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome.
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DOI：
10.1093/nar/gkt636
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发表时间：
2013-10
影响因子：
14.9
通讯作者：
Uchiumi T
中科院分区：
文献类型：
--
作者：
Lee KM;Yusa K;Chu LO;Yu CW;Oono M;Miyoshi T;Ito K;Shaw PC;Wong KB;Uchiumi T
核糖体侧柄在蛋白质合成过程中负责结合和募集翻译因子。真核茎由一个P0蛋白和两个拷贝的P1·P2异二聚体组成，形成P0（P1·P2）2五聚体P复合物。在这里，我们已经解决了全长P1·P2的结构，通过核磁共振光谱。P1和P2通过它们的螺旋N-末端结构域二聚化，而P1·P2的C-末端尾部是非结构化的，并且可以从二聚化结构域延伸到125 nm。15 N弛豫研究表明，C-末端尾部是柔性的，具有比N-末端结构域快得多的内部迁移率。用真核生物P0（P1·P2）2/eL 12替换原核生物L10（L7/L12）4/L11，使对天花粉蛋白（TCS）不敏感的大肠杆菌核糖体易于被TCS脱嘌呤，并发现C-末端尾区负责这种脱嘌呤作用。截短和插入研究表明，杂合核糖体的脱嘌呤依赖于C-末端尾内富含脯氨酸-丙氨酸的铰链区的长度。总之，我们提出了一个模型，招聘的TCS的肉瘤毒素蓖麻毒素环需要灵活的C-末端尾巴，和脯氨酸-丙氨酸丰富的铰链区延长这个C-末端的尾巴，使尾巴周围的核糖体扫描招聘TCS。
Lateral ribosomal stalk is responsible for binding and recruiting translation factors during protein synthesis. The eukaryotic stalk consists of one P0 protein with two copies of P1•P2 heterodimers to form a P0(P1•P2)2 pentameric P-complex. Here, we have solved the structure of full-length P1•P2 by nuclear magnetic resonance spectroscopy. P1 and P2 dimerize via their helical N-terminal domains, whereas the C-terminal tails of P1•P2 are unstructured and can extend up to ∼125 Å away from the dimerization domains. 15N relaxation study reveals that the C-terminal tails are flexible, having a much faster internal mobility than the N-terminal domains. Replacement of prokaryotic L10(L7/L12)4/L11 by eukaryotic P0(P1•P2)2/eL12 rendered Escherichia coli ribosome, which is insensitive to trichosanthin (TCS), susceptible to depurination by TCS and the C-terminal tail was found to be responsible for this depurination. Truncation and insertion studies showed that depurination of hybrid ribosome is dependent on the length of the proline-alanine rich hinge region within the C-terminal tail. All together, we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS.
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蚕核糖体茎复合物的分子解剖：茎蛋白的多个副本的作用。
影响因子：
14.9
作者：
Baba K;Tumuraya K;Tanaka I;Yao M;Uchiumi T
通讯作者：
Uchiumi T
影响因子：
2.9
作者：
ISHIMA, R;NAGAYAMA, K
通讯作者：
NAGAYAMA, K
影响因子：
3.6
作者：
Chiou JC;Li XP;Remacha M;Ballesta JP;Tumer NE
通讯作者：
Tumer NE
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