Interaction of fluorescent ATP and tRNA analogs with phenylalanyl-tRNA synthetase
DOI:
https://doi.org/10.7124/bc.00022AAbstract
Affinity modification of E. coli MRE-600 phenylalanyl-tRNA synthetase by 1,N6-etheno-adenosine-5-triphosphate (εATP) in the presence of different ligands has been investigated. ATP conversion into εATP results in the disturbance of specific contacts of nucle-otide with the ATP binding site in the enzyme. The εATP covalent attachment site is assumed To be situated in the tRNA 3'-terminus recognizing site. Fluorescent tRNAPhe analogs have been prepared by replacing adenosine 73 or 76 by 1,N6-ethenoadenosine. The activity of these analogs has been investigated in the aminoacylation. The low yield of photoinduced covalent attachment of these derivatives to phenylalanyl-tRNA synthetase is observed.References
Ivanov MV, Kost AA. Investigation of protein using etenoproizvodnyh adenine and cytosine. Usp Biol Khim. 1980; 21:112-9.
Paulsen H, Wintermeyer W. Incorporation of 1,N6-ethenoadenosine into the 3' terminus of tRNA using T4 RNA ligase. 1. Preparation of yeast tRNAPhe derivatives. Eur J Biochem. 1984;138(1):117-23.
Paulsen H, Wintermeyer W. Incorporation of 1,N6-ethenoadenosine into the 3' terminus of tRNA using T4 RNA ligase. 2. Preparation and ribosome interaction of fluorescent Escherichia coli tRNAMetf. Eur J Biochem. 1984;138(1):125-30.
Podust VN, Nevinsky GA, Lavrik OI. Modification of E. coli phenylalanyl-tRNA synthetase by l,N6-ethenoadenosine-5'-triphosphate. Biopolym. Cell. 1985; 1(5):267-70.
Ankilova VN, Lavrik OI, Khodyreva SN. Purification and properties of phenylalanyl-tRNA-synthetase from Escherichia coli MRE-600. Prikl Biokhim Mikrobiol. 1984;20(2):208-16.
Barrio JR, Barrio MC, Leonard NJ, England TE, Uhlenbeck OC. Synthesis of modified nucleoside 3',5'-bisphosphates and their incorporation into oligoribonucleotides with T4 RNA ligase. Biochemistry. 1978;17(11):2077-81.
Nevinsky GA, Podust VN, Ankilova VN, Lavrik OI. Phenylalanyl-tRNA synthetase from E. coli: enzyme modification by chemically reactive analogs of fluorescent nucleotides. Russian Journal of Bioorganic Chemistry. 1983; 9 (7):936-946.
Gorshkova II, Datsii II, Lavrik OI. Role of arginine residues in phenylalanyl-tRNA synthetase interaction with substrates. Mol Biol (Mosk). 1980;14(1):118-25.
Shugart L. Effect of selective chemical modification of 4-thiouridine of phenylalanine transfer ribonucleic acid on enzyme recognition. Arch Biochem Biophys. 1972;148(2):488-95.
Bartmann P, Hanke T, Holler E. Active site stoichiometry of L-phenylalanine: tRNA ligase from Escherichia coli K(-10). J Biol Chem. 1975;250(19):7668-74.
Nevinskii GA, Podust VN, Khodyreva SN, Gorshkova II, Lavrik OI. Adenosine- and ethenoadenosine-5'-trimetaphosphates: the effect of covalent bond formation on the state of the affinity label in the complex with phenylalanyl-tRNA-synthetase. Mol Biol (Mosk). 1984;18(5):1311-5.
Lavrik OI, Nevinsky GA. Phenylalanyl-tRNA synthetase from Escherichia coli MRE-600. Activation by nucleotides and affinity modification of the effector binding sites. FEBS Lett. 1980;109(1):13-7.
Tal J, Deutscher MP, Littauer UZ. Biological activity of Escherichia coli tRNA Phe modified in its C-C-A terminus. Eur J Biochem. 1972;28(4):478-91.
Holler E, Baltzinger M, Favre A. Catalytic mechanism of phenylalanyl-tRNA synthetase of Escherichia coli K10. Different properties of native and photochemically cross-linked tRNAPhe can be explained in the light of tRNA conformer equilibria. Biochemistry. 1981;20(5):1139-47.
