Evidence for dispensable sequences inserted into a nucleotide fold.
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[1] B. Low. Formation of merodiploids in matings with a class of Rec- recipient strains of Escherichia coli K12. , 1968, Proceedings of the National Academy of Sciences of the United States of America.
[2] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[3] D. Cassio,et al. Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme. , 1971, European journal of biochemistry.
[4] P. Berg,et al. Isoleucine Auxotrophy as a Consequence of a Mutationally Altered Isoleucyl-Transfer Ribonucleic Acid Synthetase , 1971, Journal of bacteriology.
[5] Anders Liljas,et al. 2 Evolutionary and Structural Relationships among Dehydrogenases , 1975 .
[6] M. Kula,et al. Labelling of L-isoleucine tRNA ligase from Escherichia coli with L-isoleucyl-bromomethyl ketone. , 1976, European Journal of Biochemistry.
[7] P. Y. Chou,et al. Empirical predictions of protein conformation. , 1978, Annual review of biochemistry.
[8] A. Sancar,et al. Simple method for identification of plasmid-coded proteins , 1979, Journal of bacteriology.
[9] H. Towbin,et al. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[10] M S Waterman,et al. Identification of common molecular subsequences. , 1981, Journal of molecular biology.
[11] R. Doolittle. Similar amino acid sequences: chance or common ancestry? , 1981, Science.
[12] J. Risler,et al. Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases , 1981, Nature.
[13] J. Ebel,et al. Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment. , 2005, European journal of biochemistry.
[14] J. Risler,et al. Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution. , 1982, Journal of molecular biology.
[15] J. Walker,et al. Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold. , 1982, The EMBO journal.
[16] P. Brick,et al. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold. , 1982, Journal of molecular biology.
[17] G. Winter,et al. The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus. , 1983, European journal of biochemistry.
[18] T. Bhat,et al. Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetases. , 1983, Journal of molecular biology.
[19] M. Tokunaga,et al. Isolation and characterization of an Escherichia coli clone overproducing prolipoprotein signal peptidase. , 1983, The Journal of biological chemistry.
[20] L. Regan,et al. Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase , 1983, Nature.
[21] T. Webster,et al. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. , 1984, Science.
[22] S. Blanquet,et al. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene , 1984, Journal of bacteriology.
[23] F. Fuller-Pace,et al. Genetic recombination can generate altered restriction specificity. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[24] L. Regan,et al. Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site , 1984, Cell.
[25] F. Lederer,et al. Methionyl-tRNA synthetase from Escherichia coli: primary structure at the binding site for the 3'-end of tRNAfMet. , 1985, Biochemistry.
[26] T. Bickle,et al. A hybrid recognition sequence in a recombinant restriction enzyme and the evolution of DNA sequence specificity , 1985, Nature.
[27] F. Lederer,et al. Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3'-end of tRNA. , 1986, Biochemistry.
[28] P. Dessen,et al. Sequence similarities among the family of aminoacyl-tRNA synthetases. , 1986, Biochimie.
[29] P. Schimmel,et al. Internal structural features of E. coli glycyl-tRNA synthetase examined by subunit polypeptide chain fusions. , 1986, The Journal of biological chemistry.
[30] Structure of the yeast valyl-tRNA synthetase gene (VASI) and the homology of its translated amino acid sequence with Escherichia coli isoleucyl-tRNA synthetase. , 1987, The Journal of biological chemistry.
[31] S. Yokoyama,et al. Functions of isolated domains of methionyl-tRNA synthetase from an extreme thermophile, Thermus thermophilus HB8. , 1987, The Journal of biological chemistry.
[32] P. Schimmel,et al. Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. , 1987, Annual review of biochemistry.
[33] A. Fersht,et al. The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli. , 1987, Biochemistry.
[34] L. Regan,et al. Polypeptide sequences essential for RNA recognition by an enzyme. , 1987, Science.