tRNA concentration fine tunes protein solubility

被引：61

作者：

Fedyunin, Ivan ^{[1
,2
]}

Lehnhardt, Lothar ^{[1
]}

Boehmer, Nadine ^{[1
]}

Kaufmann, Paul ^{[1
]}

Zhang, Gong ^{[1
]}

Ignatova, Zoya ^{[1
]}

机构：

[1] Univ Potsdam, Inst Biochem & Biol, D-14476 Potsdam, Germany

[2] Max Planck Inst Colloids & Interfaces, IMPRS Grad Sch, D-14424 Potsdam, Germany

来源：

FEBS LETTERS | 2012年 / 586卷 / 19期

关键词：

Protein translation; Protein misfolding; tRNA; E; coli; ESCHERICHIA-COLI; CODON USAGE; TRANSLATIONAL ELONGATION; NASCENT POLYPEPTIDE; TRIGGER FACTOR; RIBOSOME; GENOME; BIAS; DETERMINANTS; ATTENUATION;

D O I：

10.1016/j.febslet.2012.07.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Clusters of codons pairing to low-abundance tRNAs synchronize the translation with co-translational folding of single domains in multidomain proteins. Although proven with some examples, the impact of the ribosomal speed on the folding and solubility on a global, cell-wide level remains elusive. Here we show that upregulation of three low-abundance tRNAs in Escherichia coli increased the aggregation propensity of several cellular proteins as a result of an accelerated elongation rate. Intriguingly, alterations in the concentration of the natural tRNA pool compromised the solubility of various chaperones consequently rendering the solubility of some chaperone-dependent proteins. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3336 / 3340

页数：5

共 35 条

[11] RESIDUAL TRANSFER-RNA SECONDARY STRUCTURE IN DENATURING 8M UREA/TBE POLYACRYLAMIDE GELS - EFFECTS ON ELECTROPHORETIC MOBILITY AND DEPENDENCY ON PRIOR CHEMICAL MODIFICATION OF THE TRANSFER-RNA [J].

HEGG, LA ;

THURLOW, DL .

NUCLEIC ACIDS RESEARCH, 1990, 18 (10) :2993-3000

[12] GENOME-WIDE TRANSLATIONAL PROFILING BY RIBOSOME FOOTPRINTING [J].

Ingolia, Nicholas T. .

METHODS IN ENZYMOLOGY, VOL 470: GUIDE TO YEAST GENETICS:: FUNCTIONAL GENOMICS, PROTEOMICS, AND OTHER SYSTEMS ANALYSIS, 2ND EDITION, 2010, 470 :119-142

[13] Divergent stalling sequences sense and control cellular physiology [J].

Ito, Koreaki ;

Chiba, Shinobu ;

Pogliano, Kit .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2010, 393 (01) :1-5

[14] Revisiting the codon adaptation index from a whole-genome perspective: analyzing the relationship between gene expression and codon occurrence in yeast using a variety of models [J].

Jansen, R ;

Bussemaker, HJ ;

Gerstein, M .

NUCLEIC ACIDS RESEARCH, 2003, 31 (08) :2242-2251

[15] A "silent" polymorphism in the MDR1 gene changes substrate specificity [J].

Kimchi-Sarfaty, Chava ;

Oh, Jung Mi ;

Kim, In-Wha ;

Sauna, Zuben E. ;

Calcagno, Anna Maria ;

Ambudkar, Suresh V. ;

Gottesman, Michael M. .

SCIENCE, 2007, 315 (5811) :525-528

[16] Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation [J].

Komar, AA ;

Lesnik, T ;

Reiss, C .

FEBS LETTERS, 1999, 462 (03) :387-391

[17] A pause for thought along the co-translational folding pathway [J].

Komar, Anton A. .

TRENDS IN BIOCHEMICAL SCIENCES, 2009, 34 (01) :16-24

[18] Codon bias as a factor in regulating expression via translation rate in the human genome [J].

Lavner, Y ;

Kotlar, D .

GENE, 2005, 345 (01) :127-138

[19] Translationally optimal codons associate with aggregation-prone sites in proteins [J].

Lee, Yaelim ;

Zhou, Tong ;

Tartaglia, Gian Gaetano ;

Vendruscolo, Michele ;

Wilke, Claus O. .

PROTEOMICS, 2010, 10 (23) :4163-4171

[20] The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria [J].

Li, Gene-Wei ;

Oh, Eugene ;

Weissman, Jonathan S. .

NATURE, 2012, 484 (7395) :538-U172

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