| Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE. | |
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MedLine Citation:
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PMID: 17419738 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The proteins CcmA and CcmB have long been known to be essential for cytochrome c maturation in Escherichia coli. We have purified a complex of these proteins, and found it to have ATP hydrolysis activity. CcmA, which has the features of a soluble ATP hydrolysis subunit, is found in a membrane-bound complex only when CcmB is present in the membrane. Mutation of the Walker A motif in CcmA(K40D) results in loss of the in vitro ATPase activity and in loss of cytochrome c biogenesis in vivo. The same mutation does not prevent covalent attachment of heme to the heme chaperone CcmE, but holo-CcmE is, for some unidentified reason, incompetent for heme transfer to an apocytochrome c or for release into the periplasm as a soluble variant. Addition of exogenous heme to heme-permeable E. coli with a ccmA deletion did not restore cytochrome c production. Our results suggest a role for CcmAB in the handling of heme by CcmE, which is chemically complex and involves an unusual histidine-heme covalent bond. |
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Authors:
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Olaf Christensen; Edgar M Harvat; Linda Thöny-Meyer; Stuart J Ferguson; Julie M Stevens |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2007-04-05 |
Journal Detail:
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Title: The FEBS journal Volume: 274 ISSN: 1742-464X ISO Abbreviation: FEBS J. Publication Date: 2007 May |
Date Detail:
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Created Date: 2007-04-23 Completed Date: 2007-06-20 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101229646 Medline TA: FEBS J Country: England |
Other Details:
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Languages: eng Pagination: 2322-32 Citation Subset: IM |
Affiliation:
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Institut für Mikrobiologie, Eidgenössische Technische Hochschule, Zürich, Switzerland. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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ATP-Binding Cassette Transporters
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biosynthesis,
chemistry,
genetics*,
metabolism Adenosine Triphosphate / metabolism* Amino Acid Motifs / genetics Aspartic Acid / genetics Bacterial Outer Membrane Proteins / biosynthesis, chemistry, genetics*, metabolism* Cytochromes c / biosynthesis, genetics, metabolism* Escherichia coli / enzymology, genetics Escherichia coli Proteins / biosynthesis, genetics, metabolism* Heme / metabolism Hemeproteins / biosynthesis, genetics, metabolism* Histidine / metabolism Hydrolysis Lysine / genetics Mutagenesis, Site-Directed* Protein Processing, Post-Translational* / genetics Protein Subunits / chemistry, genetics, metabolism Sequence Deletion |
| Chemical | |
Reg. No./Substance:
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0/ATP-Binding Cassette Transporters; 0/Bacterial Outer Membrane Proteins; 0/CcmA protein, bacteria; 0/CcmB protein, E coli; 0/CcmE protein, E coli; 0/Escherichia coli Proteins; 0/Hemeproteins; 0/Protein Subunits; 14875-96-8/Heme; 56-65-5/Adenosine Triphosphate; 56-84-8/Aspartic Acid; 56-87-1/Lysine; 71-00-1/Histidine; 9007-43-6/Cytochromes c |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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