The N‐terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl‐tRNA synthetase (TyrRSapm) is a monomer in solution. Issue 6 (4th February 2013)

• Record Type: Journal Article
• Authors: Choudhury, Aparajita; Banerjee, Rajat
• Is Part Of: FEBS letters. Volume 587:Issue 6(2013)
• Page Start: 590
• Page End: 599
• Publication Date: 2013-02-04
• Subjects: TyrRSapm -- Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase -- ΔTyrRSapm -- N-terminal domain of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase -- aa -- amino acid -- AUC -- analytical ultracentrifuge -- DTNB -- 5, 5′-dithio-bis(2-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; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.01.048
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : TyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) Abstract : ► Tyrosyl‐tRNA synthetase of mimivirus (TyrRSapm ) forms weak dimers in solution. ► N‐terminal TyrRSapm (ΔTyrRSapm ) of mimivirus exists as a monomer in solution. ► The ligand‐binding affinity forl ‐Tyr and ATP is not affected in ΔTyrRSapm, but is decreased 40‐fold for tRNA Tyr .