Nanoparticles Associate with Intrinsically Disordered RNA-Binding Proteins

被引:14
|
作者
Romashchenko, Alexander V. [1 ,2 ]
Kan, Tsung-Wai [4 ]
Petrovski, Dmitry V. [1 ,5 ]
Gerlinskaya, Ludmila A. [1 ]
Moshkin, Mikhail P. [1 ]
Moshkin, Yuri M. [1 ,3 ]
机构
[1] SB RAS, Inst Cytol & Genet, Fed Res Ctr, Novosibirsk 630090, Russia
[2] SB RAS, Inst Computat Tech, Novosibirsk 630090, Russia
[3] SB RAS, Inst Mol & Cellular Biol, Novosibirsk 630090, Russia
[4] Erasmus MC, Dept Biochem, NL-3015 CE Rotterdam, Netherlands
[5] SB RAS, Inst Systemat & Ecol Anim, Novosibirsk 630091, Russia
基金
俄罗斯科学基金会;
关键词
nanoparticles; proteomics; RNA-binding proteins; stress granules; intrinsically disordered proteins; SOLID LIPID NANOPARTICLES; PLASMA-PROTEINS; ENGINEERED NANOPARTICLES; SURFACE-CHEMISTRY; STRESS GRANULES; DRUG TRANSPORT; CELL; ADSORPTION; SIZE; PREDICTION;
D O I
10.1021/acsnano.6b05992
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Nanoparticles are capable of penetrating cells, but little is known about the way they interact with intracellular proteome. Here we show that inorganic nanoparticles associate with low-complexity, intrinsically disordered proteins from HeLa cytosolic protein extracts in nondenaturing in vitro nanoparticle pull-down assays. Intrinsic protein disorder associates with structural mobility, suggesting that side-chain flexibility plays an important role in the driving of a protein to nanoparticle absorption. Disordered protein domains are often found in a diverse group of RNA-binding proteins. Consequently, the nano particle-associated proteomes were enriched in subunits of RNA-processing protein complexes. In turn, this indicates that within a cell, nanoparticles might interfere with protein synthesis triggering a range of cellular responses.
引用
收藏
页码:1328 / 1339
页数:12
相关论文
共 50 条
  • [1] Intrinsically disordered electronegative clusters improve stability and binding specificity of RNA-binding proteins
    Zaharias, Steve
    Zhang, Zihan
    Davis, Kenneth
    Fargason, Talia
    Cashman, Derek
    Yu, Tao
    Zhang, Jun
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2021, 297 (02)
  • [2] Intrinsically disordered electronegative clusters improve stability and binding specificity of RNA-binding proteins
    Zhang, Jun
    [J]. FASEB JOURNAL, 2021, 35
  • [3] Emerging Roles of Disordered Sequences in RNA-Binding Proteins
    Calabretta, Sara
    Richard, Stephane
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2015, 40 (11) : 662 - 672
  • [4] The binding mechanisms of intrinsically disordered proteins
    Dogan, Jakob
    Gianni, Stefano
    Jemth, Per
    [J]. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2014, 16 (14) : 6323 - 6331
  • [5] Stabilization of Intrinsically Disordered DKK2 Protein by Fusion to RNA-Binding Domain
    Lee, Hye Min
    Kwon, Soon Bin
    Son, Ahyun
    Kim, Doo Hyun
    Kim, Kyun-Hwan
    Lim, Jonghyo
    Kwon, Young-Guen
    Kang, Jin Sun
    Lee, Byung Kyu
    Byun, Young Ho
    Seong, Baik L.
    [J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2019, 20 (11)
  • [6] Engineered binding proteins to amyloidogenic intrinsically disordered proteins
    Shaykhalishahi, Hamed
    Mirecka, Ewa
    Gauhar, Aziz
    Gruening, Clara
    Woerdehoff, Michael
    Feuerstein, Sophie
    Stoldt, Matthias
    Haerd, Torleif
    Willbold, Dieter
    Hoyer, Wolfgang
    [J]. PROTEIN SCIENCE, 2015, 24 : 123 - 123
  • [7] Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes
    Sobel, SG
    Wolin, SL
    [J]. MOLECULAR BIOLOGY OF THE CELL, 1999, 10 (11) : 3849 - 3862
  • [8] RNA-binding proteins in RNA interference
    Kotelnikov R.N.
    Shpiz S.G.
    Kalmykova A.I.
    Gvozdev V.A.
    [J]. Molecular Biology, 2006, 40 (4) : 528 - 540
  • [9] Binding cavities and druggability of intrinsically disordered proteins
    Zhang, Yugang
    Cao, Huaiqing
    Liu, Zhirong
    [J]. PROTEIN SCIENCE, 2015, 24 (05) : 688 - 705
  • [10] Reconciling binding mechanisms of intrinsically disordered proteins
    Michel Espinoza-Fonseca, L.
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2009, 382 (03) : 479 - 482