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本文引用的文献

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Internal initiation: IRES elements of picornaviruses and hepatitis c virus.内部起始：微小核糖核酸病毒和丙型肝炎病毒的内部核糖体进入位点元件
Virus Res. 2006 Jul;119(1):2-15. doi: 10.1016/j.virusres.2005.11.003. Epub 2005 Dec 27.
2
An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites.一种RNA相互作用蛋白，SYNCRIP（不均一核核糖核蛋白Q1/NSAP1）是一种mRNA颗粒的组成成分，它与1,4,5-三磷酸肌醇受体1型mRNA一起在神经元树突中运输。
J Biol Chem. 2004 Dec 17;279(51):53427-34. doi: 10.1074/jbc.M409732200. Epub 2004 Oct 8.
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A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon.一种细胞RNA结合蛋白通过与丙型肝炎病毒多聚蛋白起始密码子下游的相互作用增强内部核糖体进入位点依赖性翻译。
Mol Cell Biol. 2004 Sep;24(18):7878-90. doi: 10.1128/MCB.24.18.7878-7890.2004.
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Kinesin transports RNA: isolation and characterization of an RNA-transporting granule.驱动蛋白运输RNA：一种RNA运输颗粒的分离与鉴定
Neuron. 2004 Aug 19;43(4):513-25. doi: 10.1016/j.neuron.2004.07.022.
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Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein.蛋白激酶A磷酸化调节多嘧啶序列结合蛋白的转运。
Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8776-81. doi: 10.1073/pnas.1432696100. Epub 2003 Jul 8.
6
Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner.不均一核核糖核蛋白C以细胞周期阶段依赖性方式调节c-myc信使核糖核酸的翻译。
Mol Cell Biol. 2003 Jan;23(2):708-20. doi: 10.1128/MCB.23.2.708-720.2003.
7
ELAV/Hu proteins inhibit p27 translation via an IRES element in the p27 5'UTR.ELAV/Hu蛋白通过p27 5'非翻译区中的内部核糖体进入位点元件抑制p27的翻译。
Genes Dev. 2002 Dec 1;16(23):3087-99. doi: 10.1101/gad.248902.
8
Stress granules: sites of mRNA triage that regulate mRNA stability and translatability.应激颗粒：调节mRNA稳定性和可翻译性的mRNA分类场所。
Biochem Soc Trans. 2002 Nov;30(Pt 6):963-9. doi: 10.1042/bst0300963.
9
Continuous heat shock enhances translational initiation directed by internal ribosomal entry site.持续热休克增强由内部核糖体进入位点介导的翻译起始。
Biochem Biophys Res Commun. 2002 Sep 20;297(2):224-31. doi: 10.1016/s0006-291x(02)02154-x.
10
Identification of pp68 as the Tyrosine-phosphorylated Form of SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein.鉴定pp68为SYNCRIP/NSAP1的酪氨酸磷酸化形式。一种细胞质RNA结合蛋白。
J Biol Chem. 2002 Jul 12;277(28):25233-8. doi: 10.1074/jbc.M202556200. Epub 2002 May 6.

BiP内部核糖体进入位点活性受NSAP1热诱导相互作用的控制。

BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1.

作者信息

Cho Sungchan, Park Sung Mi, Kim Tae Don, Kim Jong Heon, Kim Kyong-Tai, Jang Sung Key

机构信息

Department of Life Science, Pohang University of Science and Technology, San 31, Hyoja Dong, Pohang, Kyungbuk 790-784, Republic of Korea.

出版信息

Mol Cell Biol. 2007 Jan;27(1):368-83. doi: 10.1128/MCB.00814-06. Epub 2006 Oct 30.

DOI:10.1128/MCB.00814-06
PMID:17074807
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1800651/
Abstract

TheBiP protein, a stress response protein, plays an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' nontranslated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed. Here we report that NSAP1 specifically enhances the IRES activity of BiP mRNA by interacting with the IRES element. Overexpression of NSAP1 in 293T cells increased the IRES activity of BiP mRNA, whereas knockdown of NSAP1 by small interfering RNA (siRNA) reduced the IRES activity of BiP mRNA. The amount of NSAP1 bound to the BiP IRES increased under heat stress conditions, and the IRES activity of BiP mRNA was increased. Moreover, the increase in BiP IRES activity with heat treatment was not observed in cells lacking NSAP1 after siRNA treatment. BiP mRNAs were redistributed from the heavy polysome to the light polysome in NSAP1 knockdown cells. Together, these data indicate that NSAP1 modulates IRES-dependent translation of BiP mRNA through an RNA-protein interaction under heat stress conditions.

摘要

BiP蛋白是一种应激反应蛋白，在新生蛋白质的正确折叠和组装以及内质网腔中错误折叠蛋白质的清除过程中发挥着重要作用。BiP的翻译由BiP mRNA 5'非翻译区中的内部核糖体进入位点（IRES）指导。当细胞受到热应激时，BiP IRES活性会增加。在此我们报告，NSAP1通过与IRES元件相互作用特异性增强BiP mRNA的IRES活性。在293T细胞中过表达NSAP1可增加BiP mRNA的IRES活性，而通过小干扰RNA（siRNA）敲低NSAP1则会降低BiP mRNA的IRES活性。在热应激条件下，与BiP IRES结合的NSAP1量增加，且BiP mRNA的IRES活性增强。此外，在siRNA处理后缺乏NSAP1的细胞中未观察到热处理导致的BiP IRES活性增加。在NSAP1敲低的细胞中，BiP mRNA从重多核糖体重新分布到轻多核糖体。总之，这些数据表明，在热应激条件下，NSAP1通过RNA-蛋白质相互作用调节BiP mRNA的IRES依赖性翻译。