Biology:Regulator of CO metabolism

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Short description: Heme protein transcription factor


Regulator of CO Metabolism (RcoM) is a heme-containing transcription factor found in bacteria that senses carbon monoxide (CO). In the presence of carbon monoxide, this protein upregulates expression of genes involved in carbon monoxide oxidation or carbon monoxide stress response.[1] RcoM is functionally related to another heme-containing transcription factor, CooA, but RcoM shares no structural relationship with CooA. RcoM is composed of an N-terminal Per-Arnt-Sim (PAS) domain and a C-terminal LytTR domain. The PAS domain binds a single molecule of heme and the LytTR domain binds to DNA upstream of carbon monoxide oxidation genes.[2] The RcoM homolog from Paraburkholderia xenovorans is known to be dimeric[3] and binds heme using a histidine and a methionine ligand in the Fe(II) oxidation state.[4] Carbon monoxide replaces the methionine ligand and binds directly to the heme to active RcoM for DNA binding. Relative to other heme-containing proteins, RcoM has an extraordinarily high CO affinity, with a Kd < 100 pM, allowing this protein to sense very low levels of carbon monoxide.[5]

References

  1. ↑ Kerby, Robert L.; Youn, Hwan; Roberts, Gary P. (May 2008). "RcoM: A New Single-Component Transcriptional Regulator of CO Metabolism in Bacteria" (in en). Journal of Bacteriology 190 (9): 3336–3343. doi:10.1128/JB.00033-08. ISSN 0021-9193. PMID 18326575. 
  2. ↑ Kerby, Robert L.; Roberts, Gary P. (November 2012). "Burkholderia xenovorans RcoM Bx -1, a Transcriptional Regulator System for Sensing Low and Persistent Levels of Carbon Monoxide" (in en). Journal of Bacteriology 194 (21): 5803–5816. doi:10.1128/JB.01024-12. ISSN 0021-9193. PMID 22923594. 
  3. ↑ Dent, Matthew R.; Roberts, Madeleine G.; Bowman, Hannah E.; Weaver, Brian R.; McCaslin, Darrell R.; Burstyn, Judith N. (2022-04-19). "Quaternary Structure and Deoxyribonucleic Acid-Binding Properties of the Heme-Dependent, CO-Sensing Transcriptional Regulator Px RcoM" (in en). Biochemistry 61 (8): 678–688. doi:10.1021/acs.biochem.2c00086. ISSN 0006-2960. PMID 35394749. https://pubs.acs.org/doi/10.1021/acs.biochem.2c00086. 
  4. ↑ Bowman, Hannah E.; Dent, Matthew R.; Burstyn, Judith N. (July 2016). "Met104 is the CO-replaceable ligand at Fe(II) heme in the CO-sensing transcription factor BxRcoM-1" (in en). Journal of Biological Inorganic Chemistry 21 (4): 559–569. doi:10.1007/s00775-016-1368-5. ISSN 0949-8257. PMID 27283195. http://link.springer.com/10.1007/s00775-016-1368-5. 
  5. ↑ Bouzhir-Sima, Latifa; Motterlini, Roberto; Gross, Julia; Vos, Marten H.; Liebl, Ursula (2016-10-20). "Unusual Dynamics of Ligand Binding to the Heme Domain of the Bacterial CO Sensor Protein RcoM-2" (in en). The Journal of Physical Chemistry B 120 (41): 10686–10694. doi:10.1021/acs.jpcb.6b08160. ISSN 1520-6106. PMID 27661620. https://pubs.acs.org/doi/10.1021/acs.jpcb.6b08160. 




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