Footprinting evidence for close contacts of the yeast tRNA(Asp) anticodon region with aspartyl-tRNA synthetase.
Chemical footprinting experiments on brewer's yeast tRNA(Asp) complexed to its cognate aspartyl-tRNA synthetase are reported: they demonstrate that bases of the anticodon loop, including the anticodon itself, are in close proximity with the synthetase. Contacts were determined using dimethylsulfate as the probe for testing reactivity of guanine and cytosine residues in free and complexed tRNA. Results correlate with the decrease in aspartylation activity of yeast tRNA(Asp) molecules mutated at these contact positions and will be compared with other structural data arising from solution and crystallographic studies on the aspartic acid complex.
Garcia
A
A
Unité Propre de Recherche Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance, Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France.
Giege
R
R
D000478:Alkylation; D000926:Anticodon / Q000378:metabolism*; D001226:Aspartate-tRNA Ligase / Q000378:metabolism*; D001483:Base Sequence; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012349:RNA, Transfer, Asp / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D013463:Sulfuric Acid Esters / Q000378:metabolism / Q000494:pharmacology
D000926:Anticodon; D012349:RNA, Transfer, Asp; D013463:Sulfuric Acid Esters; D001226:Aspartate-tRNA Ligase; C007482:dimethyl sulfate