Evidence for a conformational change in the exit site of the Escherichia coli ribosome upon tRNA binding

Biochemistry ◽  
1993 ◽  
Vol 32 (15) ◽  
pp. 4067-4072 ◽  
Author(s):  
J. Stephen Lodmell ◽  
William E. Tapprich ◽  
Walter E. Hill
Keyword(s):  
Escherichia Coli ◽  
Conformational Change ◽  
Exit Site ◽  
Trna Binding

scholarly journals Proteins at the tRNA Binding Sites of Escherichia coli Ribosomes

1974 ◽  
Vol 71 (1) ◽  
pp. 230-234 ◽  
Author(s):  
A. P. Czernilofsky ◽  
E. E. Collatz ◽  
G. Stoffler ◽  
E. Kuechler
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Trna Binding

scholarly journals Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme

2009 ◽  
Vol 191 (24) ◽  
pp. 7614-7619 ◽  
Author(s):  
Rong Shi ◽  
Magda Villarroya ◽  
Rafael Ruiz-Partida ◽  
Yunge Li ◽  
Ariane Proteau ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Conformational Changes ◽  
Function Analysis ◽  
Trna Modification ◽  
Conserved Residues ◽  
Limited Trypsinolysis ◽  
Fad Binding ◽  
Trna Binding

ABSTRACT The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-Å resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.

scholarly journals A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system

FEBS Journal ◽  
2005 ◽  
Vol 272 (11) ◽  
pp. 2773-2783 ◽  
Author(s):  
Tomoaki Kato ◽  
Daizo Hamada ◽  
Takashi Fukui ◽  
Makoto Hayashi ◽  
Takeshi Honda ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Conformational Change ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Escherichia Coli O157 ◽  
Type Iii ◽  
Ph Dependent

[45] Parameters for the preparation of Escherichia coli ribosomes and ribosomal subunits active in tRNA binding

1988 ◽  
pp. 658-670 ◽  
Author(s):  
Hans-Jörg Rheinberger ◽  
Ute Geigenmüller ◽  
Markus Wedde ◽  
Knud H. Nierhaus
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Subunits ◽  
Trna Binding

Affinities of tRNA binding sites of ribosomes from Escherichia coli

Biochemistry ◽  
1986 ◽  
Vol 25 (11) ◽  
pp. 3245-3255 ◽  
Author(s):  
Roland Lill ◽  
James M. Robertson ◽  
Wolfgang Wintermeyer
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Trna Binding

scholarly journals Enhancement of the Synthesis of RpoE and StpA by Polyamines at the Level of Translation in Escherichia coli under Heat Shock Conditions

2009 ◽  
Vol 191 (17) ◽  
pp. 5348-5357 ◽  
Author(s):  
Yusuke Terui ◽  
Kyohei Higashi ◽  
Yuzuru Tabei ◽  
Hideyuki Tomitori ◽  
Kaneyoshi Yamamoto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Change ◽  
Heat Shock ◽  
Cell Growth ◽  
Initiation Site ◽  
Initiation Codon ◽  
Shock Response ◽  
Common Position ◽  
Trna Binding ◽  
Stimulation Of

ABSTRACT Proteins whose synthesis is enhanced by polyamines at the level of translation were identified with a polyamine-requiring mutant cultured in the presence of 0.1% glucose and 0.02% glutamate at 42°C. Polyamines had a greater effect on cell growth at 42°C than at 37°C. At 42°C, the synthesis of RpoE (σ24) and StpA, which are involved in the transcription of a number of heat shock response genes, was stimulated by polyamines at the level of translation. In the rpoE and stpA mRNAs, a Shine-Dalgarno (SD) sequence is located at 13 and 12 nucleotides, respectively, upstream of the initiation codon AUG. When the SD sequences were moved to the more common position 7 nucleotides upstream of the initiation codon AUG, the degree of polyamine stimulation was reduced, although the level of RpoE and StpA synthesis was markedly increased. The mechanism underlying polyamine stimulation of RpoE synthesis was then studied. Polyamine stimulation of RpoE synthesis was reduced by changing the bulged-out structure in the initiation site of rpoE mRNA, although the level of RpoE synthesis increased. A selective structural change of this bulged-out region induced by spermidine at 42°C was observed by circular dichroism. Polyamine stimulation of fMet-tRNA binding to ribosomes at 42°C also disappeared by changing the bulged-out structure in the initiation site of rpoE mRNA. The results suggest that polyamines enhance the synthesis of RpoE by changing the bulged-out structure in the initiation site of rpoE mRNA.

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