Difference between revisions of "Part:BBa K1897002"

 
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<partinfo>BBa_K1897002 short</partinfo>
 
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HasR is the membrane-bound receptor in the Has system, a heme acquisition system originally from the Serratia marcescens. The HasR protein is involved in binding with a heme-loaded HasA hemophore to trigger downstream HasS and HasI. It has been shown that the N terminal of HasR is especially crucial for signal transduction. With the heme-loaded hasA bound to hasR, it induces a conformational change in HasR that causes the activation of HasS, an anti-sigma factor. HasS then releases HasI (sigma factor) that was initially bound to it and HasI ultimately is able to trigger expression of genes under control of pHas (part number).
 
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===Usage and Biology===
 
===Usage and Biology===
  
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HasR is a 98.22 kDa membrane-bound receptor in the Has system, a heme acquisition system originally from the Serratia marcescens. The HasR protein is involved in binding with a heme-loaded holo-HasA hemophore to trigger downstream signalling events. The signal transduction fails to occur with exposure to haem or the apo-HasA (Rossi et al., 2003). Furthermore, it has been shown that the N terminal of HasR is especially crucial for signal transduction (Biville Et al., 2004). With the holo-hasA bound to hasR, it induces a conformational change in HasR that causes the activation of HasS, an anti-sigma factor. HasS then releases HasI (sigma factor) initially bound to it and HasI ultimately is able to trigger expression of genes under control of pHas (BBa_K1897006).
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K1897002 SequenceAndFeatures</partinfo>
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Biville, F., Cwerman, H., Létoffé, S., Rossi, M. S., Drouet, V., Ghigo, J. M., & Wandersman, C. (2004). Haemophore‐mediated signalling in Serratia marcescens: a new mode of regulation for an extra cytoplasmic function (ECF) sigma factor involved in haem acquisition. Molecular microbiology, 53(4), 1267-1277.
  
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===Functional Parameters===
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Rossi, M. S., Paquelin, A., Ghigo, J. M., & Wandersman, C. (2003). Haemophore‐mediated signal transduction across the bacterial cell envelope in Serratia marcescens: the inducer and the transported substrate are different molecules. Molecular microbiology, 48(6), 1467-1480.
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<partinfo>BBa_K1897002 parameters</partinfo>
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K1897002 SequenceAndFeatures</partinfo>

Revision as of 21:09, 9 October 2016


HasR Membrane receptor coding sequence

Usage and Biology

HasR is a 98.22 kDa membrane-bound receptor in the Has system, a heme acquisition system originally from the Serratia marcescens. The HasR protein is involved in binding with a heme-loaded holo-HasA hemophore to trigger downstream signalling events. The signal transduction fails to occur with exposure to haem or the apo-HasA (Rossi et al., 2003). Furthermore, it has been shown that the N terminal of HasR is especially crucial for signal transduction (Biville Et al., 2004). With the holo-hasA bound to hasR, it induces a conformational change in HasR that causes the activation of HasS, an anti-sigma factor. HasS then releases HasI (sigma factor) initially bound to it and HasI ultimately is able to trigger expression of genes under control of pHas (BBa_K1897006).

Biville, F., Cwerman, H., Létoffé, S., Rossi, M. S., Drouet, V., Ghigo, J. M., & Wandersman, C. (2004). Haemophore‐mediated signalling in Serratia marcescens: a new mode of regulation for an extra cytoplasmic function (ECF) sigma factor involved in haem acquisition. Molecular microbiology, 53(4), 1267-1277.


Rossi, M. S., Paquelin, A., Ghigo, J. M., & Wandersman, C. (2003). Haemophore‐mediated signal transduction across the bacterial cell envelope in Serratia marcescens: the inducer and the transported substrate are different molecules. Molecular microbiology, 48(6), 1467-1480.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NotI site found at 1866
    Illegal NotI site found at 2660
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 24
    Illegal NgoMIV site found at 28
    Illegal NgoMIV site found at 84
    Illegal NgoMIV site found at 202
    Illegal NgoMIV site found at 356
    Illegal NgoMIV site found at 421
    Illegal NgoMIV site found at 757
  • 1000
    COMPATIBLE WITH RFC[1000]