Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms.
The specific aminoacylation of tRNA by tyrosyl-tRNA synthetases (TyrRSs) relies on the identity determinants in the cognate tRNA(Tyr)s. We have determined the crystal structure of Saccharomyces cerevisiae TyrRS (SceTyrRS) complexed with a Tyr-AMP analog and the native tRNA(Tyr)(GPsiA). Structural information for TyrRS-tRNA(Tyr) complexes is now full-line for three kingdoms. Because the archaeal/eukaryotic TyrRSs-tRNA(Tyr)s pairs do not cross-react with their bacterial counterparts, the recognition modes of the identity determinants by the archaeal/eukaryotic TyrRSs were expected to be similar to each other but different from that by the bacterial TyrRSs. Interestingly, however, the tRNA(Tyr) recognition modes of SceTyrRS have both similarities and differences compared with those in the archaeal TyrRS: the recognition of the C1-G72 base pair by SceTyrRS is similar to that by the archaeal TyrRS, whereas the recognition of the A73 by SceTyrRS is different from that by the archaeal TyrRS but similar to that by the bacterial TyrRS. Thus, the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNA(Tyr) pairs most probably lies in the different sequence of the last base pair of the acceptor stem (C1-G72 vs G1-C72) of tRNA(Tyr). On the other hand, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms.
Tsunoda
Masaru
M
School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Kusakabe
Yoshio
Y
Tanaka
Nobutada
N
Ohno
Satoshi
S
Nakamura
Masashi
M
Senda
Toshiya
T
Moriguchi
Tomohisa
T
Asai
Norio
N
Sekine
Mitsuo
M
Yokogawa
Takashi
T
Nishikawa
Kazuya
K
Nakamura
Kazuo T
KT
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000926:Anticodon / Q000737:chemistry; D019843:Archaeal Proteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D001483:Base Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D012365:RNA, Transfer, Tyr / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D016415:Sequence Alignment; D014443:Tyrosine / Q000737:chemistry; D014448:Tyrosine-tRNA Ligase / Q000737:chemistry*
D000926:Anticodon; D019843:Archaeal Proteins; D001426:Bacterial Proteins; D012365:RNA, Transfer, Tyr; D029701:Saccharomyces cerevisiae Proteins; D014443:Tyrosine; D014448:Tyrosine-tRNA Ligase