PMID:8973166: 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.125035.X52239b6994666-->
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="X52239b6994666"  class=" tableEdit PMID_info_table" 


<span style = 'font-size: large'> '''Chamberlin, M and Julin, DA'''  (1996) Interactions of the RecBCD enzyme from Escherichia coli and its subunits with DNA, elucidated from the kinetics of ATP and DNA hydrolysis with oligothymidine substrates.''Biochemistry'' '''35''':15949-61</span>
{|{{Prettytable}} align = 'center' width= '70%'
|-
|-
|{{TableHeadingColor}} |'''Abstract''' || Oligothymidines eight nucleotides or longer stimulate ATP hydrolysis by the RecBC and RecBCD enzymes, and they are substrates for the ATP-stimulated nuclease activity of RecBCD. The steady-state kinetics of ATP hydrolysis by the RecBC enzyme are consistent with a single ATPase and DNA binding site. Results with RecBCD and RecBCD-K177Q [an enzyme with a Lys-to-Gln mutation in the ATP binding motif of the RecD subunit [Korangy, F., & Julin, D. A. (1992) J. Biol. Chem. 267, 1727-1732]] indicate that ATP hydrolysis by the RecB subunit is stimulated by pd(T)12 binding to a high-affinity site, while the RecD subunit hydrolyzes ATP stimulated by pd(T)12 binding to a low-affinity site. The site which stimulates RecB has about 50-fold greater affinity for DNA in either RecBCD or RecBCD-K177Q than does the corresponding site in RecBC. The rates of ATP hydrolysis observed for the RecBCD enzyme at low concentrations of pd(T)12 are best explained by a mechanism where the enzyme binds to the DNA and catalyzes multiple rounds of ATP hydrolysis before dissociating. Larger DNA molecules [pd(T)25-30 and poly(dT)] are bound more tightly by RecBCD, are hydrolyzed more rapidly, and are much more effective in stimulating ATP hydrolysis than is pd(T)12. The results at low ATP concentrations where the nuclease activity is minimal (5 microM) suggest that ATP hydrolysis is stimulated by the DNA ends, but there is no evidence that the RecBCD enzyme moves along these DNA molecules in an ATP-dependent manner under these conditions.
!align=left  |Citation
</noinclude>
||
'''Chamberlin, M and Julin, DA'''  (1996) Interactions of the RecBCD enzyme from Escherichia coli and its subunits with DNA, elucidated from the kinetics of ATP and DNA hydrolysis with oligothymidine substrates. ''Biochemistry'' '''35''':15949-61
|-
!align=left  |Abstract
||
Oligothymidines eight nucleotides or longer stimulate ATP hydrolysis by the RecBC and RecBCD enzymes, and they are substrates for the ATP-stimulated nuclease activity of RecBCD. The steady-state kinetics of ATP hydrolysis by the RecBC enzyme are consistent with a single ATPase and DNA binding site. Results with RecBCD and RecBCD-K177Q [an enzyme with a Lys-to-Gln mutation in the ATP binding motif of the RecD subunit [Korangy, F., & Julin, D. A. (1992) J. Biol. Chem. 267, 1727-1732]] indicate that ATP hydrolysis by the RecB subunit is stimulated by pd(T)12 binding to a high-affinity site, while the RecD subunit hydrolyzes ATP stimulated by pd(T)12 binding to a low-affinity site. The site which stimulates RecB has about 50-fold greater affinity for DNA in either RecBCD or RecBCD-K177Q than does the corresponding site in RecBC. The rates of ATP hydrolysis observed for the RecBCD enzyme at low concentrations of pd(T)12 are best explained by a mechanism where the enzyme binds to the DNA and catalyzes multiple rounds of ATP hydrolysis before dissociating. Larger DNA molecules [pd(T)25-30 and poly(dT)] are bound more tightly by RecBCD, are hydrolyzed more rapidly, and are much more effective in stimulating ATP hydrolysis than is pd(T)12. The results at low ATP concentrations where the nuclease activity is minimal (5 microM) suggest that ATP hydrolysis is stimulated by the DNA ends, but there is no evidence that the RecBCD enzyme moves along these DNA molecules in an ATP-dependent manner under these conditions.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8973166 PubMed]
Online version:[http://dx.doi.org/10.1021/bi961643n 10.1021/bi961643n]
|-
|-
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8973166 PubMed]
!align=left  |Keywords
||
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; DNA/metabolism; Endodeoxyribonucleases/chemistry; Endodeoxyribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Exodeoxyribonuclease V; Exodeoxyribonucleases/chemistry; Exodeoxyribonucleases/metabolism; Kinetics; Macromolecular Substances; Models, Chemical; Oligodeoxyribonucleotides/metabolism; Substrate Specificity
 
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.125035.X52239b6994666&page=125035&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
|}
</protect>
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.125035.X52239b6994666-->
==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.W47aa8182984a7-->
<annotationlinks/>
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|class = 'sortable' {{Prettytable}} id='232730'
|- {{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.W47aa8182984a7&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
<!--box uid=63ce1649aab8b3180235b0af7618f667.0.W47aa8182984a7--></protect>


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

Latest revision as of 04:56, 15 September 2013

Citation

Chamberlin, M and Julin, DA (1996) Interactions of the RecBCD enzyme from Escherichia coli and its subunits with DNA, elucidated from the kinetics of ATP and DNA hydrolysis with oligothymidine substrates. Biochemistry 35:15949-61

Abstract

Oligothymidines eight nucleotides or longer stimulate ATP hydrolysis by the RecBC and RecBCD enzymes, and they are substrates for the ATP-stimulated nuclease activity of RecBCD. The steady-state kinetics of ATP hydrolysis by the RecBC enzyme are consistent with a single ATPase and DNA binding site. Results with RecBCD and RecBCD-K177Q [an enzyme with a Lys-to-Gln mutation in the ATP binding motif of the RecD subunit [Korangy, F., & Julin, D. A. (1992) J. Biol. Chem. 267, 1727-1732]] indicate that ATP hydrolysis by the RecB subunit is stimulated by pd(T)12 binding to a high-affinity site, while the RecD subunit hydrolyzes ATP stimulated by pd(T)12 binding to a low-affinity site. The site which stimulates RecB has about 50-fold greater affinity for DNA in either RecBCD or RecBCD-K177Q than does the corresponding site in RecBC. The rates of ATP hydrolysis observed for the RecBCD enzyme at low concentrations of pd(T)12 are best explained by a mechanism where the enzyme binds to the DNA and catalyzes multiple rounds of ATP hydrolysis before dissociating. Larger DNA molecules [pd(T)25-30 and poly(dT)] are bound more tightly by RecBCD, are hydrolyzed more rapidly, and are much more effective in stimulating ATP hydrolysis than is pd(T)12. The results at low ATP concentrations where the nuclease activity is minimal (5 microM) suggest that ATP hydrolysis is stimulated by the DNA ends, but there is no evidence that the RecBCD enzyme moves along these DNA molecules in an ATP-dependent manner under these conditions.

Links

PubMed Online version:10.1021/bi961643n

Keywords

Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; DNA/metabolism; Endodeoxyribonucleases/chemistry; Endodeoxyribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Exodeoxyribonuclease V; Exodeoxyribonucleases/chemistry; Exodeoxyribonucleases/metabolism; Kinetics; Macromolecular Substances; Models, Chemical; Oligodeoxyribonucleotides/metabolism; Substrate Specificity

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:8973166&oldid=1473142"