Physicochemical studies of YB-1 functions and structures

YB-1功能和结构的理化研究

• 批准号: 24750166
• 负责人: NAGATOISHI Satoru
• 金额: $ 2.91万
• 依托单位: The University of Tokyo
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Young Scientists (B)
• 财政年份: 2012
• 资助国家: 日本
• 起止时间: 2012-04-01 至 2014-03-31
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-24750166/
• 关键词: 天然変性型蛋白質; 熱力学; 相互作用; 核酸; 天然変性蛋白質; 物理化学解析; 溶媒和

Y-box binding protein 1(YB-1) is a nucleic acid-binding protein that regulates transcription and translation, and is overexpressed in cancer cells. It has been reported that the bindings of YB-1 to specific genomic DNAs or mRNAs are involved in tumorigenesis. Therefore, it is plausible to suppose that YB-1 is a new target to regulate the cellular systems due to treatment of human diseases and elucidation of new cellular functions. However, the binding mechanism of YB-1 to nucleic acids is still unclear. Here, we carried out physicochemical analyses of the structural and binding properties of YB-1 using spectrometry and calorimetry. The recombinant YB-1 had thermodynamically unique bindings to the single-strand DNA with Y-box sequence and to the single-strand DNA with Y-box mRNA sequence. The DNA and RNA binding sites of YB-1 were identified by using a full length and deletion mutants of YB-1. We further studied the effects of salt and temperature on the binding to DNA or RNA.

Y-box binding protein 1（YB-1）是一种调节转录和翻译的核酸结合蛋白，在癌细胞中过表达。据报道，YB-1与特定基因组dna或mrna的结合参与了肿瘤的发生。因此，我们有理由认为，由于治疗人类疾病和阐明新的细胞功能，YB-1是调节细胞系统的新靶点。然而，YB-1与核酸的结合机制尚不清楚。本文采用分光光度法和量热法对YB-1的结构和结合特性进行了理化分析。重组蛋白YB-1与含有Y-box序列的单链DNA和含有Y-box mRNA序列的单链DNA具有独特的热力学结合。利用YB-1全长突变体和缺失突变体鉴定了YB-1的DNA和RNA结合位点。我们进一步研究了盐和温度对其与DNA或RNA结合的影响。

项目成果

Physicochemical studies of YB-1 functions and structures

YB-1功能和结构的理化研究

• 发表时间: 2013
• 作者: Satoru Nagatoishi;Yumiko Tanabe;Kouhei Tsumoto
• 通讯作者: Kouhei Tsumoto

生命分子相互作用解析 : ITCとSPR

生物分子相互作用分析：ITC 和 SPR

• 发表时间: 2014
• 作者: 長門石曉;津本浩平
• 通讯作者: 津本浩平

Effects of a thymine residue deletion in TT loops on thrombin-TBA recognition interactions: a crystallographic study

TT 环中胸腺嘧啶残基缺失对凝血酶-TBA 识别相互作用的影响：晶体学研究

• 发表时间: 2012
• 作者: I. R. Kraussa;A Picaa;A. Merlinoa;S. Nagatoishi;N. Sugimoto;L;Mazzarella and F. Sica
• 通讯作者: Mazzarella and F. Sica

Interaction of water with the G-quadruplex loop contributes to the binding energy of G-quadruplex to protein

水与 G-四链体环的相互作用有助于 G-四链体与蛋白质的结合能

• DOI: 10.1039/c2mb25234a
• 发表时间: 2012
• 期刊: Mol. Biosyst.
• 作者: S. Nakano;H. Hirayama;D. Miyoshi and N. Sugimoto;S. Nagatoishi and N. Sugimoto
• 通讯作者: S. Nagatoishi and N. Sugimoto

Dissecting the contribution of thrombin exosite I in the recognition of thrombin binding aptamer

• DOI: 10.1111/febs.12561
• 发表时间: 2013-12-01
• 期刊: FEBS JOURNAL
• 影响因子: 5.4
• 作者: Pica, Andrea;Russo Krauss, Irene;Sica, Filomena
• 通讯作者: Sica, Filomena