Abstract：
:The steps of UUC recognition by tRNAPhe were analysed by temperature-jump measurements. At ion concentrations close to physiological conditions we found three relaxation processes, which we assigned to (1) formation of codon-anticodon complexes, (2) a conformational change of the anticodon loop coupled with Mg2+ binding, and (3) codon-induced association of tRNA. The relaxation data were evaluated both by the usual procedure (fitting the exponentials evaluated from the individual experiments of a set to a reaction model) and by "global fitting", i.e. fitting a set of relaxation curves obtained at various concentrations directly to a reaction model, thus leaving out the intermediate exponential fitting step. The data can be represented quantitatively by a three-step model: the codon binds to the anticodon at a rate of 4 X 10(6) to 6 X 10(6) M-1S-1 as is usual for the formation of oligomer helices; the conformation change of the anticodon loop is associated with inner sphere complexation of Mg2+ at a rate of 10(3) S-1; the codon-tRNA complexes form dimers at a rate of 5 X 10(6) to 15 X 10(6) M-1S-1. A similar mechanism is found for the binding of the wobble codon UUU to tRNAPhe at increased concentrations of Mg2+. Measurements at different Mg2+ concentrations demonstrate the distinct role of this ion in the codon recognition and the codon-induced tRNA dimerization. We propose a simple mechanism, based upon the special properties of magnesium ions, for long-distance transfer of reaction signals along nucleic acid chains.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Labuda D,Striker G,Porschke Ddoi
10.1016/0022-2836(84)90085-8subject
Has Abstractpub_date
1984-04-25 00:00:00pages
587-604issue
4eissn
0022-2836issn
1089-8638pii
0022-2836(84)90085-8journal_volume
174pub_type
杂志文章abstract：:We describe a method for probing the integrity and relative orientation of structural elements that are indirectly linked by ligands in protein complexes during protein folding. The effect of 3'-GMP on the rate constants of unfolding of wild-type barnase and several mutants has been studied. By comparing the rates of ...
journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1016/0022-2836(91)80188-z
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journal_title：Journal of molecular biology
pub_type： 杂志文章
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更新日期：1991-12-05 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1006/jmbi.1998.1672
更新日期：1998-04-24 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1006/jmbi.1995.0486
更新日期：1995-09-15 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1006/jmbi.1999.2553
更新日期：1999-03-12 00:00:00
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pub_type： 杂志文章
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1016/j.jmb.2009.06.042
更新日期：2009-08-14 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
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更新日期：2007-10-19 00:00:00
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journal_title：Journal of molecular biology
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journal_title：Journal of molecular biology
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更新日期：2009-01-23 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1006/jmbi.1993.1473
更新日期：1993-08-20 00:00:00
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pub_type： 杂志文章
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更新日期：2003-02-07 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
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更新日期：2006-08-18 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1016/0022-2836(86)90021-5
更新日期：1986-12-20 00:00:00
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pub_type： 杂志文章,评审
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journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1016/0022-2836(92)90553-v
更新日期：1992-04-05 00:00:00
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journal_title：Journal of molecular biology
pub_type： 杂志文章,评审
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更新日期：2019-11-22 00:00:00
abstract：:Here, we have investigated the specificity of purified recombinant tRNA:m(2)(2)G10 methyltransferase of Pyrococcus abyssi ((Pab)Trm-m(2)(2)G10 enzyme). This archaeal enzyme catalyses mono- and dimethylation of the N(2)-exocyclic amino group of guanine at position 10 of several tRNA species. Our results indicate that o...
journal_title：Journal of molecular biology
pub_type： 杂志文章
doi：10.1016/j.jmb.2005.12.087
更新日期：2006-03-24 00:00:00
