Difference between revisions of "Part:BBa K4242004"

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===Usage and Biology===
 
===Usage and Biology===
 
YedQ can work with the phosphodiesterase (YhjH) modulated the in vivo c-di-GMP levels. The expression of the yedQ gene increased the intracellular c-di-GMP concentration and resulted in the enhanced secretion of EPS[1]. So, The protein YedQ can promote bacterial self-aggregation and adhesion onto negatively charged surfaces. In <i>E. coli</i>, extracellular DNA (eDNA) was increased as expected for the deletions of yedQ. As a result of the significantly enhanced motility, but contrary to current models of decreased biofilm formation with decreased diguanylate cyclase activity, early biofilm formation increased dramatically for the deletions of yedQ[2].  
 
YedQ can work with the phosphodiesterase (YhjH) modulated the in vivo c-di-GMP levels. The expression of the yedQ gene increased the intracellular c-di-GMP concentration and resulted in the enhanced secretion of EPS[1]. So, The protein YedQ can promote bacterial self-aggregation and adhesion onto negatively charged surfaces. In <i>E. coli</i>, extracellular DNA (eDNA) was increased as expected for the deletions of yedQ. As a result of the significantly enhanced motility, but contrary to current models of decreased biofilm formation with decreased diguanylate cyclase activity, early biofilm formation increased dramatically for the deletions of yedQ[2].  
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<h3><center>FleQ protein bend with DNA</center></h3>
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<div class = "center">
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<center>https://static.igem.org/mediawiki/parts/c/c2/Model_of_pel_regulation_under_the_FleQ.jpeg </center>
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</div>
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<center>* Baraquet C <i>et al</i>. Nucleic Acids Res, 2012.</center>
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<center><b>Figure 1:</b> Model of <i>pel</i> regulation. FleQ binds to two FleQ boxes on the <i>pel</i> promoter (A). FleQ interacts with FleN in the absence of ATP (B) as well as in the presence of ATP, but in this case, it induces a distortion of <i>pel</i> DNA (C). We propose that FleN forms a bridge between two FleQ bound to their binding sites. The binding of FleQ to FleQ box 2 is essential for repression. The binding of c-di-GMP to FleQ induces a conformational change of FleQ, probably propagated through FleN, which induces the relief of <i>pel</i> distortion and leads to <i>pel</i> expression (D). The binding of FleQ to FleQ box 1 is essential for activation[3].</center>
  
 
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Revision as of 15:32, 8 October 2022


yedQ

This part sequence originated from Escherichia coli encodes YedQ protein. YedQ is diguanylate cyclase.

Usage and Biology

YedQ can work with the phosphodiesterase (YhjH) modulated the in vivo c-di-GMP levels. The expression of the yedQ gene increased the intracellular c-di-GMP concentration and resulted in the enhanced secretion of EPS[1]. So, The protein YedQ can promote bacterial self-aggregation and adhesion onto negatively charged surfaces. In E. coli, extracellular DNA (eDNA) was increased as expected for the deletions of yedQ. As a result of the significantly enhanced motility, but contrary to current models of decreased biofilm formation with decreased diguanylate cyclase activity, early biofilm formation increased dramatically for the deletions of yedQ[2].

FleQ protein bend with DNA

Model_of_pel_regulation_under_the_FleQ.jpeg
* Baraquet C et al. Nucleic Acids Res, 2012.
Figure 1: Model of pel regulation. FleQ binds to two FleQ boxes on the pel promoter (A). FleQ interacts with FleN in the absence of ATP (B) as well as in the presence of ATP, but in this case, it induces a distortion of pel DNA (C). We propose that FleN forms a bridge between two FleQ bound to their binding sites. The binding of FleQ to FleQ box 2 is essential for repression. The binding of c-di-GMP to FleQ induces a conformational change of FleQ, probably propagated through FleN, which induces the relief of pel distortion and leads to pel expression (D). The binding of FleQ to FleQ box 1 is essential for activation[3].

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 1591
  • 1000
    COMPATIBLE WITH RFC[1000]

References

[1] Yang S, Wu Y, Qu C, et al. Quantitative analysis of the surficial and adhesion properties of the Gram-negative bacterial species Comamonas testosteroni modulated by c-di-GMP[J]. Colloids Surf B Biointerfaces, 2021,198:111497.

[2] Sanchez-Torres V, Hu H, Wood T K. GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and swimming motility in Escherichia coli[J]. Appl Microbiol Biotechnol, 2011,90(2):651-658.