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The N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution

TyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) ► Tyrosyl‐tRNA synthetase of mimivirus (TyrRS) forms weak dimers in solution. ► N‐terminal TyrRS (ΔTyrRS) of mimivirus exists as a monomer in solution. ► The ligand‐binding affinity for ‐Tyr and ATP is not affected in ΔTyrRS, b... Full description

Journal Title: FEBS Letters 18 March 2013, Vol.587(6), pp.590-599
Main Author: Choudhury, Aparajita
Other Authors: Banerjee, Rajat
Format: Electronic Article Electronic Article
Language:
Subjects:
Aa
Auc
5
Dtt
Sds
Cd
ID: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2013.01.048
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recordid: wj10.1016/j.febslet.2013.01.048
title: The N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution
format: Article
creator:
  • Choudhury, Aparajita
  • Banerjee, Rajat
subjects:
  • Tyrrs Apm
  • Acanthamoeba Polyphaga Mimivirus Tyrosyl-Trna Synthetase
  • Δtyrrs Apm
  • N-Terminal Domain Of Acanthamoeba Polyphaga Mimivirus Tyrosyl-Trna Synthetase
  • Aa
  • Amino Acid
  • Auc
  • Analytical Ultracentrifuge
  • Dtnb
  • 5
  • 5′-Dithio-Bis2-Nitrobenzoic Acid
  • Dtt
  • Dithiothreotrol
  • Sds
  • Sodium Dodecyl Sulphate
  • Gdnhcl
  • Guanidine Hydrochloride
  • Cd
  • Circular Dichroism
  • Mimivirus Tyrosyl-Trna Synthetase
  • Trna
  • Monomer
  • Analytical Ultracentrifuge
  • Dissociation Constant
  • Disulfide-Bridge
ispartof: FEBS Letters, 18 March 2013, Vol.587(6), pp.590-599
description: TyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) ► Tyrosyl‐tRNA synthetase of mimivirus (TyrRS) forms weak dimers in solution. ► N‐terminal TyrRS (ΔTyrRS) of mimivirus exists as a monomer in solution. ► The ligand‐binding affinity for ‐Tyr and ATP is not affected in ΔTyrRS, but is decreased 40‐fold for tRNA.
language:
source:
identifier: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2013.01.048
fulltext: fulltext
issn:
  • 0014-5793
  • 00145793
  • 1873-3468
  • 18733468
url: Link


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titleThe N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution
creatorChoudhury, Aparajita ; Banerjee, Rajat
ispartofFEBS Letters, 18 March 2013, Vol.587(6), pp.590-599
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subjectTyrrs Apm ; Acanthamoeba Polyphaga Mimivirus Tyrosyl-Trna Synthetase ; Δtyrrs Apm ; N-Terminal Domain Of Acanthamoeba Polyphaga Mimivirus Tyrosyl-Trna Synthetase ; Aa ; Amino Acid ; Auc ; Analytical Ultracentrifuge ; Dtnb ; 5 ; 5′-Dithio-Bis2-Nitrobenzoic Acid ; Dtt ; Dithiothreotrol ; Sds ; Sodium Dodecyl Sulphate ; Gdnhcl ; Guanidine Hydrochloride ; Cd ; Circular Dichroism ; Mimivirus Tyrosyl-Trna Synthetase ; Trna ; Monomer ; Analytical Ultracentrifuge ; Dissociation Constant ; Disulfide-Bridge
descriptionTyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) ► Tyrosyl‐tRNA synthetase of mimivirus (TyrRS) forms weak dimers in solution. ► N‐terminal TyrRS (ΔTyrRS) of mimivirus exists as a monomer in solution. ► The ligand‐binding affinity for ‐Tyr and ATP is not affected in ΔTyrRS, but is decreased 40‐fold for tRNA.
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titleThe N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution
descriptionTyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) ► Tyrosyl‐tRNA synthetase of mimivirus (TyrRS) forms weak dimers in solution. ► N‐terminal TyrRS (ΔTyrRS) of mimivirus exists as a monomer in solution. ► The ligand‐binding affinity for ‐Tyr and ATP is not affected in ΔTyrRS, but is decreased 40‐fold for tRNA.
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105′-Dithio-Bis2-Nitrobenzoic Acid
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titleThe N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution
authorChoudhury, Aparajita ; Banerjee, Rajat
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105′-Dithio-Bis2-Nitrobenzoic Acid
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atitleThe N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution
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abstractTyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) ► Tyrosyl‐tRNA synthetase of mimivirus (TyrRS) forms weak dimers in solution. ► N‐terminal TyrRS (ΔTyrRS) of mimivirus exists as a monomer in solution. ► The ligand‐binding affinity for ‐Tyr and ATP is not affected in ΔTyrRS, but is decreased 40‐fold for tRNA.
doi10.1016/j.febslet.2013.01.048
pages590-599
date2013-03-18