Domain-domain communication in aminoacyl-tRNA synthetases

[51] A SIMPLE STRUCTURAL FEATURE IS A MAJOR DETERMINANT OF THE IDENTITY OF A TRANSFER-RNA [J]. NATURE, 1988, 333 (6169) : 140 - 145

[52] ESCHERICHIA-COLI TYROSYL-TRANSFER RNA AND METHIONYL-TRANSFER RNA-SYNTHETASES DISPLAY SEQUENCE SIMILARITY AT THE BINDING-SITE FOR THE 3'-END OF TRANSFER-RNA [J]. BIOCHEMISTRY, 1986, 25 (01) : 16 - 21

[53] Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (14) : 6953 - 6958

[54] A euryarchaeal Lysyl-tRNA synthetase: Resemblance to class I synthetases [J]. SCIENCE, 1997, 278 (5340) : 1119 - 1122

[55] Ilyin VA, 2000, PROTEIN SCI, V9, P218

[56] ANTICODON AND ACCEPTOR STEM NUCLEOTIDES IN TRANSFER RNAGLN ARE MAJOR RECOGNITION ELEMENTS FOR ESCHERICHIA-COLI GLUTAMINYL-TRANSFER RNA-SYNTHETASE [J]. NATURE, 1991, 352 (6332) : 258 - 260

[57] MODULAR ARRANGEMENT OF FUNCTIONAL DOMAINS ALONG THE SEQUENCE OF AN AMINOACYL TRANSFER-RNA SYNTHETASE [J]. NATURE, 1983, 306 (5942) : 441 - 447

[58] DISPENSABLE PIECES OF AN AMINOACYL TRANSFER-RNA SYNTHETASE WHICH ACTIVATE THE CATALYTIC SITE [J]. CELL, 1984, 36 (04) : 1089 - 1095

[59] JASIN M, 1985, J BIOL CHEM, V260, P2226

[60] 2 SEPARATE PEPTIDES IN ESCHERICHIA-COLI METHIONYL-TRANSFER RNA-SYNTHETASE FORM THE ANTICODON BINDING-SITE FOR METHIONINE TRANSFER-RNA [J]. BIOCHEMISTRY, 1993, 32 (39) : 10506 - 10511

[51] A SIMPLE STRUCTURAL FEATURE IS A MAJOR DETERMINANT OF THE IDENTITY OF A TRANSFER-RNA [J]. NATURE, 1988, 333 (6169) : 140 - 145

[52] ESCHERICHIA-COLI TYROSYL-TRANSFER RNA AND METHIONYL-TRANSFER RNA-SYNTHETASES DISPLAY SEQUENCE SIMILARITY AT THE BINDING-SITE FOR THE 3'-END OF TRANSFER-RNA [J]. BIOCHEMISTRY, 1986, 25 (01) : 16 - 21

[53] Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (14) : 6953 - 6958

[54] A euryarchaeal Lysyl-tRNA synthetase: Resemblance to class I synthetases [J]. SCIENCE, 1997, 278 (5340) : 1119 - 1122

[55] Ilyin VA, 2000, PROTEIN SCI, V9, P218

[56] ANTICODON AND ACCEPTOR STEM NUCLEOTIDES IN TRANSFER RNAGLN ARE MAJOR RECOGNITION ELEMENTS FOR ESCHERICHIA-COLI GLUTAMINYL-TRANSFER RNA-SYNTHETASE [J]. NATURE, 1991, 352 (6332) : 258 - 260

[57] MODULAR ARRANGEMENT OF FUNCTIONAL DOMAINS ALONG THE SEQUENCE OF AN AMINOACYL TRANSFER-RNA SYNTHETASE [J]. NATURE, 1983, 306 (5942) : 441 - 447

[58] DISPENSABLE PIECES OF AN AMINOACYL TRANSFER-RNA SYNTHETASE WHICH ACTIVATE THE CATALYTIC SITE [J]. CELL, 1984, 36 (04) : 1089 - 1095

[59] JASIN M, 1985, J BIOL CHEM, V260, P2226

[60] 2 SEPARATE PEPTIDES IN ESCHERICHIA-COLI METHIONYL-TRANSFER RNA-SYNTHETASE FORM THE ANTICODON BINDING-SITE FOR METHIONINE TRANSFER-RNA [J]. BIOCHEMISTRY, 1993, 32 (39) : 10506 - 10511