PMID:19944692: Difference between revisions
Jump to navigation
Jump to search
New PMID: Page! |
Fill PMID: Page! |
||
| Line 1: | Line 1: | ||
{{RightTOC}} | |||
<protect> | |||
<span style = 'font-size: large'> '''Suzuki, T and Miyauchi, K''' (2009) Discovery and characterization of tRNA(Ile) lysidine synthetase (TilS).''FEBS Lett.'' </span> | |||
{|{{Prettytable}} align = 'center' width= '70%' | |||
|- | |||
|{{TableHeadingColor}} |'''Abstract''' || <protect>In the bacterial decoding system, the AUA codon is deciphered as isoleucine by tRNA(Ile) bearing lysidine (L, 2-lysyl-cytidine) at the wobble position. Lysidine is an essential modification that determines both the codon and amino acid specificities of tRNA(Ile). We identified an enzyme named tRNA(Ile) lysidine synthetase (TilS) that catalyzes lysidine formation by using lysine and ATP as substrates. Biochemical studies revealed a molecular mechanism of lysidine formation that consists of two consecutive reactions involving the adenylated tRNA intermediate. In addition, we deciphered how Escherichia coli TilS specifically discriminates between tRNA(Ile) and the structurally similar tRNA(Met), which bears the same anticodon loop. Recent structural studies unveiled tRNA recognition by TilS, and a molecular basis of lysidine formation at atomic resolution.</protect> | |||
|- | |||
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19944692 PubMed]<br/>Online version:[http://dx.doi.org/10.1016/j.febslet.2009.11.085 10.1016/j.febslet.2009.11.085] | |||
|} | |||
</protect> | |||
==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<protect><!--box uid=63ce1649aab8b3180235b0af7618f667.170022.K4b26b5ff6d871--> | |||
<!-- | |||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" | |||
|- {{table heading style}} | |||
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | |||
|-class='sortbottom' | |||
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.170022.K4b26b5ff6d871&page=170022&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || || | |||
|} | |||
<!--box uid=63ce1649aab8b3180235b0af7618f667.170022.K4b26b5ff6d871--></protect> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
{{RefHelp}} | |||
<references/> | |||
Revision as of 22:02, 14 December 2009
Suzuki, T and Miyauchi, K (2009) Discovery and characterization of tRNA(Ile) lysidine synthetase (TilS).FEBS Lett.
| Abstract | <protect>In the bacterial decoding system, the AUA codon is deciphered as isoleucine by tRNA(Ile) bearing lysidine (L, 2-lysyl-cytidine) at the wobble position. Lysidine is an essential modification that determines both the codon and amino acid specificities of tRNA(Ile). We identified an enzyme named tRNA(Ile) lysidine synthetase (TilS) that catalyzes lysidine formation by using lysine and ATP as substrates. Biochemical studies revealed a molecular mechanism of lysidine formation that consists of two consecutive reactions involving the adenylated tRNA intermediate. In addition, we deciphered how Escherichia coli TilS specifically discriminates between tRNA(Ile) and the structurally similar tRNA(Met), which bears the same anticodon loop. Recent structural studies unveiled tRNA recognition by TilS, and a molecular basis of lysidine formation at atomic resolution. |
|-
|bgcolor='#CCCCFF' nowrap |Links || PubMed
Online version:10.1016/j.febslet.2009.11.085
|}
</protect>
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| edit table |
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
See also
References
See Help:References for how to manage references in EcoliWiki.