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Physicochemical studies of YB-1 functions and structures

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:
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
项目状态:
已结题
起止时间:
2012-04-01 至 2014-03-31

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中文摘要
翻译
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。
英文摘要
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.
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DOI: --
发表时间: 2013
期刊:
影响因子: --
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
DOI: --
发表时间: 2014
期刊:
影响因子: --
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
DOI: --
发表时间: 2012
期刊:
影响因子: --
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.
影响因子: --
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
共 12 条
    Elucidation of the weak interaction-triggered system of proteins and its design proposal
    • 批准号:
      18H02082
    • 项目类别:
      Grant-in-Aid for Scientific Research (B)
    • 资助金额:
      $11.07万
    • 财政年份:
      2018
    • 负责人:
      NAGATOISHI Satoru
    • 依托单位:
    海外基金