L10 ribosomal protein from Entamoeba histolytica share structural and functional homologies with QM/Jif-1:: proteins with extraribosomal functions
L10 ribosomal protein from Entamoeba histolytica share structural and functional homologies with QM/Jif-1:: proteins with extraribosomal functions
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DOI：
10.1016/s0166-6851(02)00332-8
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发表时间：
2003-04-03
影响因子：
1.5
通讯作者：
Vargas, M
中科院分区：
文献类型：
--
作者：
Chávez-Rios, R;Arias-Romero, LE;Vargas, M
在目前的工作中，报道了溶组织内阿米巴核糖体蛋白 L10 (EhL10) 的完整氨基酸序列。 630的cDNA揭示了编码210个氨基酸的蛋白质的开放阅读框。对 EhL10 核糖体蛋白的分析显示，它与智人的 QM 蛋白有 75% 的相似性和 57% 的同一性，与拟南芥的 QM 蛋白分别有 78% 和 60% 的相似性。对溶组织内阿米巴核糖体蛋白的蛋白质印迹分析表明，EhL10 蛋白是核糖体复合物的一部分。对转染的溶组织内阿米巴菌株中EhL10分布的免疫荧光分析表明，EhL10蛋白主要定位于滋养体的细胞核。在用 pExEhNeo/EhL10 载体转染的滋养体中，EhL10 核糖体蛋白的过度表达表现出细胞生长减少 60%。 DNA 迁移率变化分析表明，EhL10 核糖体蛋白能够破坏与 c-Jun 样蛋白特异性结合的激活蛋白 1 (AP-1) 复合物的稳定性。本研究提出，EhL10与c-Jun样蛋白形成的复合物会干扰Jun控制的基因（即参与细胞生长的基因）的转录激活。据报道，使用抗这种蛋白质的人类特异性抗体，在溶组织内阿米巴核提取物中鉴定出了 AP-1 复合体的成员，即 c-Jun 样蛋白质。观察结果表明，EhL10 在溶组织内阿米巴中可能具有类似于 QM 蛋白的核糖体外功能，参与抑制溶组织内阿米巴中的细胞增殖。 (C) 2003 Elsevier Science B.V. 保留所有权利。
In the present work, the complete amino acid sequence of the Entamoeba histolytica ribosomal protein L10 (EhL10) is reported. cDNA of 630 by revealed an open reading frame that encodes a protein of 210 amino acids. Analysis of EhL10 ribosomal protein revealed 75% similarity and 57% identity with QM protein from Homo sapiens and 78 and 60%, respectively, with Arabidopsis thaliana. Western blot analysis of ribosomal proteins from E. histolytica showed that EhL10 protein is part of the ribosomal complex. Immunofluorescence analysis of EhL10 distribution in a transfected E. histolytica strain showed that EhL10 protein was mainly localized in the nucleus of trophozoites. Overexpression of EhL10 ribosomal protein in trophozoites transfected with the pExEhNeo/EhL10 vector exhibited a 60% reduction in cellular growth. DNA mobility-shift assays demonstrated that EhL10 ribosomal protein was able to destabilize the activating protein 1 (AP-1) complex binding specifically to the c-Jun-like protein. It is proposed in this study that the complex formation of EhL10 with c-Jun-like protein interferes with transcriptional activation of genes controlled by Jun (i.e. gene involved in cell growth). It is also being reported identification of a member of the AP-1 complex, the c-Jun-like protein, in nuclear extracts of E. histolytica using human-specific antibodies against this protein. The observations suggest that EhL10 may have an extraribosomal function in E. histolytica involved in suppression of cell proliferation in E. histolytica similar to the QM protein. (C) 2003 Elsevier Science B.V. All rights reserved.