Difference between revisions of "S-box Element"
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The S-box element is a [[riboswitch]] that controls different genes of sulphur metabolism in response to the presence of S-adenosylmethionine. | The S-box element is a [[riboswitch]] that controls different genes of sulphur metabolism in response to the presence of S-adenosylmethionine. | ||
* Upon binding of SAM, the [[riboswitch]] adopts a terminator structure resulting in transcription termination. | * Upon binding of SAM, the [[riboswitch]] adopts a terminator structure resulting in transcription termination. | ||
| − | * In the | + | * In the absence of SAM, the [[riboswitch]] has the antitermination structure that allows transcription elongation into the controlled gene/ operon. |
* S-box riboswitch turnover is initiated by [[rny |RNase Y]] {{PubMed|19779461}} | * S-box riboswitch turnover is initiated by [[rny |RNase Y]] {{PubMed|19779461}} | ||
| Line 18: | Line 18: | ||
==References== | ==References== | ||
| + | <pubmed> 18039762,12626738 ,17381302 19779461 12787499 18039762 18443629 20951706 22543867 28701520</pubmed> | ||
| − | + | =See also:= | |
| + | * [[RNA switch]] | ||
| + | |||
| + | =Back to [[regulons]]= | ||
Latest revision as of 09:03, 14 July 2017
The S-box element is a riboswitch that controls different genes of sulphur metabolism in response to the presence of S-adenosylmethionine.
- Upon binding of SAM, the riboswitch adopts a terminator structure resulting in transcription termination.
- In the absence of SAM, the riboswitch has the antitermination structure that allows transcription elongation into the controlled gene/ operon.
- S-box riboswitch turnover is initiated by RNase Y PubMed
Genes controlled by a S-box
- cysH-cysP-sat-cysC-ylnD-ylnE-ylnF
- metE
- metI-metC
- metK
- metN-metP-metQ
- mtnK-mtnA
- mtnW-mtnX-mtnB-mtnD
- yitJ-yitI-yitH
- yoaD-yoaC-yoaB
- yxjG
- yxjH
References
Anne-Marie Dussault, Audrey Dubé, Frédéric Jacques, Jonathan P Grondin, Daniel A Lafontaine
Ligand recognition and helical stacking formation are intimately linked in the SAM-I riboswitch regulatory mechanism.
RNA: 2017, 23(10);1539-1551
[PubMed:28701520]
[WorldCat.org]
[DOI]
(I p)
Vamsi Krishna Boyapati, Wei Huang, Jessica Spedale, Fareed Aboul-Ela
Basis for ligand discrimination between ON and OFF state riboswitch conformations: the case of the SAM-I riboswitch.
RNA: 2012, 18(6);1230-43
[PubMed:22543867]
[WorldCat.org]
[DOI]
(I p)
Changrui Lu, Fang Ding, Anirban Chowdhury, Vineeta Pradhan, Jerneja Tomsic, W Michael Holmes, Tina M Henkin, Ailong Ke
SAM recognition and conformational switching mechanism in the Bacillus subtilis yitJ S box/SAM-I riboswitch.
J Mol Biol: 2010, 404(5);803-18
[PubMed:20951706]
[WorldCat.org]
[DOI]
(I p)
Karen Shahbabian, Ailar Jamalli, Léna Zig, Harald Putzer
RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis.
EMBO J: 2009, 28(22);3523-33
[PubMed:19779461]
[WorldCat.org]
[DOI]
(I p)
Joy Xin Wang, Ronald R Breaker
Riboswitches that sense S-adenosylmethionine and S-adenosylhomocysteine.
Biochem Cell Biol: 2008, 86(2);157-68
[PubMed:18443629]
[WorldCat.org]
[DOI]
(P p)
Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762]
[WorldCat.org]
[DOI]
(I p)
T M Henkin, F J Grundy
Sensing metabolic signals with nascent RNA transcripts: the T box and S box riboswitches as paradigms.
Cold Spring Harb Symp Quant Biol: 2006, 71;231-7
[PubMed:17381302]
[WorldCat.org]
[DOI]
(P p)
Maumita Mandal, Benjamin Boese, Jeffrey E Barrick, Wade C Winkler, Ronald R Breaker
Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria.
Cell: 2003, 113(5);577-86
[PubMed:12787499]
[WorldCat.org]
[DOI]
(P p)
Brooke A Murphy McDaniel, Frank J Grundy, Irina Artsimovitch, Tina M Henkin
Transcription termination control of the S box system: direct measurement of S-adenosylmethionine by the leader RNA.
Proc Natl Acad Sci U S A: 2003, 100(6);3083-8
[PubMed:12626738]
[WorldCat.org]
[DOI]
(P p)
