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rdf:type |
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lifeskim:mentions |
umls-concept:C0005495,
umls-concept:C0010749,
umls-concept:C0018966,
umls-concept:C0030685,
umls-concept:C0220781,
umls-concept:C0243041,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C0683712,
umls-concept:C1283071,
umls-concept:C1963578
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pubmed:issue |
1
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pubmed:dateCreated |
2006-7-7
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pubmed:abstractText |
Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for cytochrome c biogenesis. Here, we show the mechanism by which the system I pathway can utilize haem at low levels. The mechanism involves an ATP-binding cassette (ABC) transporter that is required for release of the periplasmic haem chaperone CcmE to the last step of cytochrome c assembly. This ABC transporter is composed of the ABC subunit CcmA, and two membrane proteins, CcmB and CcmC. In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead-end complex, indicating high affinity binding of haem to CcmC. Expression of CcmA and CcmB facilitates formation of the CcmA2B1C1 complex and ATP-dependent release of holoCcmE. We propose that the CcmA2B1C1 complex represents a new subgroup within the ABC transporter superfamily that functions to release a chaperone.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CcmA protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/CcmB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/CcmC protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/CcmE protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
219-31
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16824107-ATP-Binding Cassette Transporters,
pubmed-meshheading:16824107-Apoproteins,
pubmed-meshheading:16824107-Bacterial Outer Membrane Proteins,
pubmed-meshheading:16824107-Bacterial Proteins,
pubmed-meshheading:16824107-Biological Transport,
pubmed-meshheading:16824107-Cytochrome c Group,
pubmed-meshheading:16824107-Escherichia coli,
pubmed-meshheading:16824107-Escherichia coli Proteins,
pubmed-meshheading:16824107-Heme,
pubmed-meshheading:16824107-Hemeproteins,
pubmed-meshheading:16824107-Membrane Proteins,
pubmed-meshheading:16824107-Models, Biological,
pubmed-meshheading:16824107-Molecular Chaperones,
pubmed-meshheading:16824107-Plasmids,
pubmed-meshheading:16824107-Recombinant Fusion Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis.
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pubmed:affiliation |
Washington University, Department of Biology Campus Box 1137, 1 Brookings Drive, St. Louis, MO 63130, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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