Document Detail


Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE.
MedLine Citation:
PMID:  17419738     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Olaf Christensen; Edgar M Harvat; Linda Thöny-Meyer; Stuart J Ferguson; Julie M Stevens
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-04-05
Journal Detail:
Title:  The FEBS journal     Volume:  274     ISSN:  1742-464X     ISO Abbreviation:  FEBS J.     Publication Date:  2007 May 
Date Detail:
Created Date:  2007-04-23     Completed Date:  2007-06-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  2322-32     Citation Subset:  IM    
Affiliation:
Institut für Mikrobiologie, Eidgenössische Technische Hochschule, Zürich, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
ATP-Binding Cassette Transporters / 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:
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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