View source for PMID:12166643

{{RightTOC}}
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.118582.P522383c6a7d6d-->
<!--
******************************************************************************************
* 
*   ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. ** 
* 
****************************************************************************************** -->
{|   id="P522383c6a7d6d"  class=" tableEdit PMID_info_table"  

|-
!align=left  |Citation
||
'''Guillier, M, Allemand, F, Raibaud, S, Dardel, F, Springer, M and Chiaruttini, C'''  (2002) Translational feedback regulation of the gene for L35 in Escherichia coli requires binding of ribosomal protein L20 to two sites in its leader mRNA: a possible case of ribosomal RNA-messenger RNA molecular mimicry. ''RNA'' '''8''':878-89
|-
!align=left  |Abstract
||
In addition to being a component of the large ribosomal subunit, ribosomal protein L20 of Escherichia coli also acts as a translational repressor. L20 is synthesized from the IF3 operon that contains three cistrons coding for IF3, and ribosomal proteins L35 and L20. L20 directly represses the expression of the gene encoding L35 and the expression of its own gene by translational coupling. All of the cis-acting sequences required for repression by L20, called the operator, are found on an mRNA segment extending from the middle of the IF3 gene to the start of the L35 gene. L20-mediated repression requires a long-range base-pairing interaction between nucleotide residues within the IF3 gene and residues just upstream of the L35 gene. This interaction results in the formation of a pseudoknot. Here we show that L20 causes protection of nucleotide residues in two regions of the operator in vitro. The first region is the pseudoknot itself and the second lies in an irregular stem located upstream of the L35 gene. By primer extension analysis, we show that L20 specifically induces reverse transcriptase stops in both regions. Therefore, these two regions define two L20-binding sites in the operator. Using mutations and deletions of rpml'-'lacZ fusions, we show that both sites are essential for repression in vivo. However L20 can bind to each site independently in vitro. One site is similar to the L20-binding site on 23S rRNA. Here we propose that L20 recognizes its mRNA and its rRNA in similar way.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12166643 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1370305 PMC1370305]

|-
!align=left  |Keywords
||
5' Untranslated Regions; Arabidopsis Proteins; Bacterial Proteins; Base Sequence; Binding Sites/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Feedback; Genes, Bacterial; Molecular Mimicry; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nucleic Acid Conformation; Operon; Plant Proteins/genetics; Protein Biosynthesis; RNA, Bacterial/chemistry; RNA, Bacterial/genetics; RNA, Bacterial/metabolism; RNA, Ribosomal/chemistry; RNA, Ribosomal/genetics; RNA, Ribosomal/metabolism; RNA, Ribosomal, 23S/genetics; RNA, Ribosomal, 23S/metabolism; Repressor Proteins/genetics; Repressor Proteins/metabolism; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Sequence Deletion

|- class="tableEdit_footer" 
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.118582.P522383c6a7d6d&page=118582&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.118582.P522383c6a7d6d-->
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<annotationlinks/>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>