TY - JOUR
T1 - A 15N-1H nuclear magnetic resonance study on the interaction between isoleucine tRNA and isoleucyl-tRNA synthetase from Escherichia coli
AU - Niimi, T.
AU - Kawai, G.
AU - Takayanagi, M.
AU - Noguchi, T.
AU - Hayashi, N.
AU - Kohno, T.
AU - Muto, Y.
AU - Watanabe, K.
AU - Miyazawa, T.
AU - Yokoyama, S.
PY - 1993
Y1 - 1993
N2 - Imino 15N and 1H resonances of Escherichia coli tRNAlIle were observed in the absence and presence of E coli isoleucyl-tRNA synthetase. Upon complex formation of tRNAlIle with isoleucyl-tRNA synthetase, some imino 15N-1H resonances disappeared, and some others were significantly broadened and/or shifted in the 1H chemical shift, while the others were observed at the same 15H-1H chemical shifts. It was indicated that the binding of tRNAlIle with IleRS affect the following four regions: the anticodon stem, the junction of the acceptor and T stems, the middle of the D stem, and the region where the tertiary base pair connects the T, D, and extra loops. This result is consistent with those of chemical footprinting and site-directed mutagenesis studies. Taken together, these three independent results reveal the recognition mechanism of tRNAlIle by IleRS: IleRS recognizes all the identity determinants distributed throughout the tRNAlIle molecule, which induces changes in the secondary and tertiary structures of tRNAlIle.
AB - Imino 15N and 1H resonances of Escherichia coli tRNAlIle were observed in the absence and presence of E coli isoleucyl-tRNA synthetase. Upon complex formation of tRNAlIle with isoleucyl-tRNA synthetase, some imino 15N-1H resonances disappeared, and some others were significantly broadened and/or shifted in the 1H chemical shift, while the others were observed at the same 15H-1H chemical shifts. It was indicated that the binding of tRNAlIle with IleRS affect the following four regions: the anticodon stem, the junction of the acceptor and T stems, the middle of the D stem, and the region where the tertiary base pair connects the T, D, and extra loops. This result is consistent with those of chemical footprinting and site-directed mutagenesis studies. Taken together, these three independent results reveal the recognition mechanism of tRNAlIle by IleRS: IleRS recognizes all the identity determinants distributed throughout the tRNAlIle molecule, which induces changes in the secondary and tertiary structures of tRNAlIle.
KW - aminoacyl-tRNA synthetase
KW - isotope labeling
KW - NMR
KW - tRNA
UR - https://www.scopus.com/pages/publications/0027788940
UR - https://www.scopus.com/inward/citedby.url?scp=0027788940&partnerID=8YFLogxK
U2 - 10.1016/0300-9084(93)90010-P
DO - 10.1016/0300-9084(93)90010-P
M3 - Article
C2 - 8199246
AN - SCOPUS:0027788940
SN - 0300-9084
VL - 75
SP - 1109
EP - 1115
JO - Biochimie
JF - Biochimie
IS - 12
ER -