Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Jack C.-H. Liu"'
Publikováno v:
RNA. 4:639-646
Escherichia coli tRNA(Val) with pyrimidine substitutions for the universally conserved 3'-terminal adenine can be readily aminoacylated. It cannot, however, transfer valine into polypeptides. Conversely, despite being a poor substrate for valyl-tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09264e06aeefbdae36cbda7af4fb1e6d
https://doi.org/10.1017/s1355838298980013
https://doi.org/10.1017/s1355838298980013
Publikováno v:
Nucleic Acids Research. 25:4883-4890
Although the anticodon is the primary element in Escherichia coli tRNAValfor recognition by valyl-tRNA synthetase (ValRS), nucleotides in the acceptor stem and other parts of the tRNA modulate recognition. Study of the steady state aminoacylation kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2c91abe4d7e099a05595408fc90f9a6
https://doi.org/10.1093/nar/25.24.4883
https://doi.org/10.1093/nar/25.24.4883
Publikováno v:
Nucleic Acids Research. 25:3944-3949
Binding of ethidium bromide to Escherichia coli tRNAVal and an RNA minihelix based on the acceptor stem and T-arm of tRNAVal was investigated by 19F and 1H NMR spectroscopy of RNAs labeled with fluorine by incorporation of 5-fluorouracil. Ethidium br
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4a91cf4797c560a8a7f93d70b026cf3
https://doi.org/10.1093/nar/25.19.3944
https://doi.org/10.1093/nar/25.19.3944
Publikováno v:
Biochemistry. 38(24)
We have studied the interactions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic footprinting with nuclease S1 and ribonuclease V1, and by analysis of the aminoacylation kinetics of mutant tRNAVal transcripts. Valyl-tR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39cf89f9e2ef0b16c21bc14d54935ca7
https://pubmed.ncbi.nlm.nih.gov/10387013
https://pubmed.ncbi.nlm.nih.gov/10387013