PMID:10954591: Difference between revisions

From EcoliWiki
Jump to navigation Jump to search
New PMID: Page!
 
imported>Wikientrybot
change PMID template to TableEdit version
 
(7 intermediate revisions by 2 users not shown)
Line 1: Line 1:
<protect>
{{RightTOC}}
{{RightTOC}}
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.120735.U52237fb5c48c4-->
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="U52237fb5c48c4"  class=" tableEdit PMID_info_table" 


<span style = 'font-size: large'> '''Shimokawa, H, Fujii, Y, Furuichi, M, Sekiguchi, M and Nakabeppu, Y'''  (2000) Functional significance of conserved residues in the phosphohydrolase module of Escherichia coli MutT protein.''Nucleic Acids Res.'' '''28''':3240-9</span>
|-
!align=left  |Citation
||
'''Shimokawa, H, Fujii, Y, Furuichi, M, Sekiguchi, M and Nakabeppu, Y'''  (2000) Functional significance of conserved residues in the phosphohydrolase module of Escherichia coli MutT protein. ''Nucleic Acids Res.'' '''28''':3240-9
|-
!align=left  |Abstract
||
Escherichia coli MutT protein hydrolyzes 8-oxo-7,8-dihydro-2'-dGTP (8-oxo-dGTP) to the monophosphate, thus avoiding the incorporation of 8-oxo-7,8-dihydroguanine (8-oxo-G) into nascent DNA. Bacterial and mammalian homologs of MutT protein share the phosphohydrolase module (MutT: Gly37-->Gly59). By saturation mutagenesis of conserved residues in the MutT module, four of the 10 conserved residues (Gly37, Gly38, Glu53 and Glu57) were revealed to be essential to suppress spontaneous A:T-->C:G transversion mutation in a mutT(-) mutator strain. For the other six residues (Lys39, Glu44, Thr45, Arg52, Glu56 and Gly59), many positive mutants which can suppress the spontaneous mutation were obtained; however, all of the positive mutants for Glu44 and Arg52 either partially or inefficiently suppressed the mutation, indicating that these two residues are also important for MutT function. Several positive mutants for Lys39, Thr45, Glu56 and Gly59 efficiently decreased the elevated spontaneous mutation rate, as seen with the wild-type, hence, these four residues are non-essential for MutT function. As Lys38 and Glu55 in human MTH1, corresponding to the non-essential residues Lys39 and Glu56 in MutT, could not be replaced by any other residue without loss of function, different structural features between the two modules of MTH1 and MutT proteins are evident.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10954591 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC110708 PMC110708]


{|{{Prettytable}} align = 'center' width= '70%'
|-
|-
|{{TableHeadingColor}} |'''Abstract''' || Escherichia coli MutT protein hydrolyzes 8-oxo-7,8-dihydro-2'-dGTP (8-oxo-dGTP) to the monophosphate, thus avoiding the incorporation of 8-oxo-7,8-dihydroguanine (8-oxo-G) into nascent DNA. Bacterial and mammalian homologs of MutT protein share the phosphohydrolase module (MutT: Gly37-->Gly59). By saturation mutagenesis of conserved residues in the MutT module, four of the 10 conserved residues (Gly37, Gly38, Glu53 and Glu57) were revealed to be essential to suppress spontaneous A:T-->C:G transversion mutation in a mutT(-) mutator strain. For the other six residues (Lys39, Glu44, Thr45, Arg52, Glu56 and Gly59), many positive mutants which can suppress the spontaneous mutation were obtained; however, all of the positive mutants for Glu44 and Arg52 either partially or inefficiently suppressed the mutation, indicating that these two residues are also important for MutT function. Several positive mutants for Lys39, Thr45, Glu56 and Gly59 efficiently decreased the elevated spontaneous mutation rate, as seen with the wild-type, hence, these four residues are non-essential for MutT function. As Lys38 and Glu55 in human MTH1, corresponding to the non-essential residues Lys39 and Glu56 in MutT, could not be replaced by any other residue without loss of function, different structural features between the two modules of MTH1 and MutT proteins are evident.
!align=left  |Keywords
</noinclude>
||
|-
Amino Acid Sequence; Amino Acid Substitution/genetics; Arginine/genetics; Arginine/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Catalytic Domain/genetics; Codon/genetics; Conserved Sequence/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Glutamic Acid/genetics; Glutamic Acid/metabolism; Glycine/genetics; Glycine/metabolism; Kinetics; Lysine/genetics; Lysine/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed/genetics; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/metabolism; Pyrophosphatases; Suppression, Genetic/genetics; Threonine/genetics; Threonine/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10954591 PubMed]
 
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.120735.U52237fb5c48c4&page=120735&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
|}
</protect>
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.120735.U52237fb5c48c4-->
==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}
Line 19: Line 38:


==Annotations {{HelpIcon|Help:Literature}}==
==Annotations {{HelpIcon|Help:Literature}}==
<protect><!--box uid=63ce1649aab8b3180235b0af7618f667.0.N47a9a1acee4ab-->
<annotationlinks/>
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|class = 'sortable' {{Prettytable}} id='228409'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.N47a9a1acee4ab&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
<!--box uid=63ce1649aab8b3180235b0af7618f667.0.N47a9a1acee4ab--></protect>


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

Latest revision as of 04:13, 15 September 2013

Citation

Shimokawa, H, Fujii, Y, Furuichi, M, Sekiguchi, M and Nakabeppu, Y (2000) Functional significance of conserved residues in the phosphohydrolase module of Escherichia coli MutT protein. Nucleic Acids Res. 28:3240-9

Abstract

Escherichia coli MutT protein hydrolyzes 8-oxo-7,8-dihydro-2'-dGTP (8-oxo-dGTP) to the monophosphate, thus avoiding the incorporation of 8-oxo-7,8-dihydroguanine (8-oxo-G) into nascent DNA. Bacterial and mammalian homologs of MutT protein share the phosphohydrolase module (MutT: Gly37-->Gly59). By saturation mutagenesis of conserved residues in the MutT module, four of the 10 conserved residues (Gly37, Gly38, Glu53 and Glu57) were revealed to be essential to suppress spontaneous A:T-->C:G transversion mutation in a mutT(-) mutator strain. For the other six residues (Lys39, Glu44, Thr45, Arg52, Glu56 and Gly59), many positive mutants which can suppress the spontaneous mutation were obtained; however, all of the positive mutants for Glu44 and Arg52 either partially or inefficiently suppressed the mutation, indicating that these two residues are also important for MutT function. Several positive mutants for Lys39, Thr45, Glu56 and Gly59 efficiently decreased the elevated spontaneous mutation rate, as seen with the wild-type, hence, these four residues are non-essential for MutT function. As Lys38 and Glu55 in human MTH1, corresponding to the non-essential residues Lys39 and Glu56 in MutT, could not be replaced by any other residue without loss of function, different structural features between the two modules of MTH1 and MutT proteins are evident.

Links

PubMed PMC110708

Keywords

Amino Acid Sequence; Amino Acid Substitution/genetics; Arginine/genetics; Arginine/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Catalytic Domain/genetics; Codon/genetics; Conserved Sequence/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Glutamic Acid/genetics; Glutamic Acid/metabolism; Glycine/genetics; Glycine/metabolism; Kinetics; Lysine/genetics; Lysine/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed/genetics; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/metabolism; Pyrophosphatases; Suppression, Genetic/genetics; Threonine/genetics; Threonine/metabolism

edit table

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

<annotationlinks/>

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.

Retrieved from "https://ecoliwiki.org/colipedia/index.php?title=PMID:10954591&oldid=1452605"