Multidrug and toxin extrusion protein 2: Difference between revisions
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== Function == |
== Function == |
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This gene encodes a protein belonging to a family of transporters involved in excretion of toxic electrolytes, both endogenous and exogenous, through urine and bile. This transporter family shares homology with the bacterial MATE ([[multi antimicrobial extrusion protein]] or multidrug and toxic compound extrusion) protein family responsible for drug resistance.<ref name="pmid9661020">{{cite journal | author = Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T | title = NorM, a Putative Multidrug Efflux Protein, of Vibrio parahaemolyticus and Its Homolog in Escherichia coli | journal = Antimicrob. Agents Chemother. | volume = 42 | issue = 7 | pages = 1778–82 | |
This gene encodes a protein belonging to a family of transporters involved in excretion of toxic electrolytes, both endogenous and exogenous, through urine and bile. This transporter family shares homology with the bacterial MATE ([[multi antimicrobial extrusion protein]] or multidrug and toxic compound extrusion) protein family responsible for drug resistance.<ref name="pmid9661020">{{cite journal | author = Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T | title = NorM, a Putative Multidrug Efflux Protein, of Vibrio parahaemolyticus and Its Homolog in Escherichia coli | journal = Antimicrob. Agents Chemother. | volume = 42 | issue = 7 | pages = 1778–82 |date=July 1998 | pmid = 9661020 | pmc = 105682 | doi = | url = }}</ref> This gene is one of two members of the MATE transporter family located near each other on chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.<ref name="entrez"/> |
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== Discovery == |
== Discovery == |
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The multidrug [[efflux (microbiology)|efflux]] [[Membrane transport protein|transporter]] '''NorM''' from ''[[Vibrio parahaemolyticus|V. parahaemolyticus]]'' which mediates resistance to multiple antimicrobial agents ([[norfloxacin]], [[kanamycin]], [[ethidium bromide]] etc.) and its homologue from ''[[Escherichia coli|E. coli]]'' were identified in 1998.<ref name="pmid9661020"/> NorM seems to function as drug/sodium [[antiporter]] which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux (microbiology)|efflux]] transporter discovered.<ref name="pmid11073914">{{cite journal | author = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of Vibrio parahaemolyticus Is an Na+-Driven Multidrug Efflux Pump | journal = J. Bacteriol. | volume = 182 | issue = 23 | pages = 6694–7 | |
The multidrug [[efflux (microbiology)|efflux]] [[Membrane transport protein|transporter]] '''NorM''' from ''[[Vibrio parahaemolyticus|V. parahaemolyticus]]'' which mediates resistance to multiple antimicrobial agents ([[norfloxacin]], [[kanamycin]], [[ethidium bromide]] etc.) and its homologue from ''[[Escherichia coli|E. coli]]'' were identified in 1998.<ref name="pmid9661020"/> NorM seems to function as drug/sodium [[antiporter]] which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux (microbiology)|efflux]] transporter discovered.<ref name="pmid11073914">{{cite journal | author = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of Vibrio parahaemolyticus Is an Na+-Driven Multidrug Efflux Pump | journal = J. Bacteriol. | volume = 182 | issue = 23 | pages = 6694–7 |date=December 2000 | pmid = 11073914 | pmc = 111412 | doi = 10.1128/JB.182.23.6694-6697.2000| url = }}</ref> NorM is a prototype of a new [[Membrane transport protein|transporter]] family and Brown ''et al''. named it the multidrug and toxic compound extrusion family.<ref name="pmid9987140">{{cite journal | author = Brown MH, Paulsen IT, Skurray RA | title = The multidrug efflux protein NorM is a prototype of a new family of transporters | journal = Mol. Microbiol. | volume = 31 | issue = 1 | pages = 394–5 |date=January 1999 | pmid = 9987140 | doi = 10.1046/j.1365-2958.1999.01162.x| url = }}</ref> The X-ray structure of the NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter.<ref name="pmid20861838">{{cite journal | author = He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G | title = Structure of a Cation-bound Multidrug and Toxic Compound Extrusion Transporter | journal = Nature | volume = 467| issue = 7318| pages = 991–4| year = 2010 | month = | pmid = 20861838 | doi = 10.1038/nature09408 | pmc = 3152480}}</ref> |
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==References== |
==References== |
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Revision as of 03:29, 30 January 2014
Template:PBB Solute carrier family 47, member 2, also known as SLC47A2, is a protein which in humans is encoded by the SLC47A2 gene.[1]
Function
This gene encodes a protein belonging to a family of transporters involved in excretion of toxic electrolytes, both endogenous and exogenous, through urine and bile. This transporter family shares homology with the bacterial MATE (multi antimicrobial extrusion protein or multidrug and toxic compound extrusion) protein family responsible for drug resistance.[2] This gene is one of two members of the MATE transporter family located near each other on chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[1]
Discovery
The multidrug efflux transporter NorM from V. parahaemolyticus which mediates resistance to multiple antimicrobial agents (norfloxacin, kanamycin, ethidium bromide etc.) and its homologue from E. coli were identified in 1998.[2] NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter discovered.[3] NorM is a prototype of a new transporter family and Brown et al. named it the multidrug and toxic compound extrusion family.[4] The X-ray structure of the NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter.[5]
References
- ^ a b "Entrez Gene: MATE2 H+/organic cation antiporter".
- ^ a b Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T (July 1998). "NorM, a Putative Multidrug Efflux Protein, of Vibrio parahaemolyticus and Its Homolog in Escherichia coli". Antimicrob. Agents Chemother. 42 (7): 1778–82. PMC 105682. PMID 9661020.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T (December 2000). "NorM of Vibrio parahaemolyticus Is an Na+-Driven Multidrug Efflux Pump". J. Bacteriol. 182 (23): 6694–7. doi:10.1128/JB.182.23.6694-6697.2000. PMC 111412. PMID 11073914.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Brown MH, Paulsen IT, Skurray RA (January 1999). "The multidrug efflux protein NorM is a prototype of a new family of transporters". Mol. Microbiol. 31 (1): 394–5. doi:10.1046/j.1365-2958.1999.01162.x. PMID 9987140.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G (2010). "Structure of a Cation-bound Multidrug and Toxic Compound Extrusion Transporter". Nature. 467 (7318): 991–4. doi:10.1038/nature09408. PMC 3152480. PMID 20861838.
{{cite journal}}: Cite has empty unknown parameter:|month=(help)CS1 maint: multiple names: authors list (link)
Further reading
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