Searching tRNA sequences for relatedness to aminoacyl-tRNA synthetase families

Hugh B. Nicholas1, William H. McClain2
1Pittsburgh Supercomputing Center, Pittsburgh, USA
2Department of Bacteriology, University of Wisconsin, Madison, USA

Tóm tắt

Từ khóa


Tài liệu tham khảo

Belrhali H, Yaremchuk A, Tukalo M, Larsen K, Berthet-Colominas C, Leberman R, Beijer B, Sproat B, Als-Nielsen J, Grübel G, Legrand J-F, Mogens M, Cusack S (1994) Crystal structure at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate. Science 263:1432–1436

Biou V, Yaremchuk A, Tukalo M, Cusack S (1994) The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer. Science 263:1404–1410

Cavarelli J, Eriani G, Rees B, Ruff M, Boeglin M, Mitschler A, Martin F, Gangloff J, Thierry J-C, Moras D (1994) The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J 13:327–337

Cavarelli J, Moras D (1993) Recognition of tRNAs by aminoacyl-tRNA synthetases. Fed Am Soc Exp Biol J 7:79–86

Eigen M, Lindemann BF, Tietze M, Winkler-Oswatitsch R, Dress A, von Haeseler A (1989) How old is the genetic code? Statistical geometry of tRNA provides an answer. Science 244:673–679

Eriani G, Delarue M, Poch O, Gangloff J, Moras D (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347:203–206

Fitch WM, Upper K (1987) The phylogeny of tRNA sequences provides evidence for ambiguity reduction in the origin of the genetic code. Cold Spring Harbor Symp Quant Biol 52:759–767

McClain WH (1993) Rules that govern tRNA identity in protein synthesis. J Mol Biol 234:257–280

McClain WH, Nicholas HB Jr (1987) Differences between transfer RNA molecules. J Mol Biol 194:635–642

Möller W, Janssen GMC (1990) Transfer RNAs for primordial amino acids contain remnants of a primitive code at positions 3 to 5. Biochimie 72:361–368

Nagel GM, Doolittle RF (1991) Evolution and relatedness in two aminoacyl-tRNA synthetase families. Proc Natl Acad Sci USA 88: 8121–8125

Nicholas HB Jr, Graves SB (1983) Clustering of transfer RNAs by cell type and amino acid specificity. J Mol Biol 171:111–118

Perona JJ, Rould MA, Steitz TA (1993) Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 32:8758–8771

Rould MA, Perona JJ, Soll D, Steitz TA (1989) Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP at 2.8Å resolution. Science 246:1135–1142

Ruff M, Krishnaswamy S, Boeglin M, Poterszman A, Mitschler A, Podjamy A, Rees B, Thierry JC, Moras D (1991) Class II aminoacyl transfer RNA synthetases: Crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNAAsp. Science 252:1682–1689

Sokal RR, Rohlf FJ (1981) Biometry. New York, pp 787–794

Sprinzl M, Hartmann T, Weber J, Blank J, Zeidler R (1989) Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res (Suppl) 17:r1-r172