The specificity of translational control switched with transfer RNA identity rules.
The interaction of Escherichia coli threonyl-transfer RNA (tRNA) synthetase with the leader sequence of its own messenger RNA inhibits ribosome binding, resulting in negative translational feedback regulation. The leader sequence resembles the substrate (tRNA(Thr)) of the enzyme, and the nucleotides that mediate the correct recognition of the leader and the tRNA may be the same. A mutation suggested by tRNA identity rules that switches the resemblance of the leader sequence from tRNA(Thr) to tRNA(Met) causes the translation of the threonyl-tRNA synthetase messenger RNA to become regulated by methionyl-tRNA synthetase. This identity swap in the leader messenger RNA indicates that tRNA identity rules may be extended to interactions of synthetases with other RNAs.
Institut de Biologie Physico-Chimique, Paris, France.
M
M
Graffe
J
J
Dondon
J
J
Caillet
P
P
Romby
C
C
Ehresmann
B
B
Ehresmann
M
M
Springer
D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D004252:DNA Mutational Analysis; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism* / Q000648:ultrastructure; D012363:RNA, Transfer, Thr / Q000378:metabolism*; D013914:Threonine-tRNA Ligase / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger; D012363:RNA, Transfer, Thr; D013914:Threonine-tRNA Ligase