PMID:17419738: Difference between revisions
New PMID: Page! |
Fill PMID: Page! |
||
| Line 1: | Line 1: | ||
{{RightTOC}} | |||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.183751.H540e6358ad55c--> | |||
<!-- | |||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{| id="H540e6358ad55c" class=" tableEdit PMID_info_table" | |||
|- | |||
!align=left |Citation | |||
|| | |||
'''Christensen, O, Harvat, EM, Thöny-Meyer, L, Ferguson, SJ and Stevens, JM''' (2007) Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE. ''FEBS J.'' '''274''':2322-32 | |||
|- | |||
!align=left |Abstract | |||
|| | |||
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. | |||
|- | |||
!align=left |Links | |||
|| | |||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17419738 PubMed] | |||
Online version:[http://dx.doi.org/10.1111/j.1742-4658.2007.05769.x 10.1111/j.1742-4658.2007.05769.x] | |||
|- | |||
!align=left |Keywords | |||
|| | |||
ATP-Binding Cassette Transporters/biosynthesis; ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/genetics; ATP-Binding Cassette Transporters/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Motifs/genetics; Aspartic Acid/genetics; Bacterial Outer Membrane Proteins/biosynthesis; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Cytochromes c/biosynthesis; Cytochromes c/genetics; Cytochromes c/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heme/metabolism; Hemeproteins/biosynthesis; Hemeproteins/genetics; Hemeproteins/metabolism; Histidine/metabolism; Hydrolysis; Lysine/genetics; Mutagenesis, Site-Directed; Protein Processing, Post-Translational/genetics; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/metabolism; Sequence Deletion | |||
|- class="tableEdit_footer" | |||
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.183751.H540e6358ad55c&page=183751&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | |||
|} | |||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.183751.H540e6358ad55c--> | |||
==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<annotationlinks/> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
{{RefHelp}} | |||
<references/> | |||
Latest revision as of 02:18, 9 September 2014
| Citation |
Christensen, O, Harvat, EM, Thöny-Meyer, L, Ferguson, SJ and Stevens, JM (2007) Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE. FEBS J. 274:2322-32 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1111/j.1742-4658.2007.05769.x |
| Keywords |
ATP-Binding Cassette Transporters/biosynthesis; ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/genetics; ATP-Binding Cassette Transporters/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Motifs/genetics; Aspartic Acid/genetics; Bacterial Outer Membrane Proteins/biosynthesis; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Cytochromes c/biosynthesis; Cytochromes c/genetics; Cytochromes c/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heme/metabolism; Hemeproteins/biosynthesis; Hemeproteins/genetics; Hemeproteins/metabolism; Histidine/metabolism; Hydrolysis; Lysine/genetics; Mutagenesis, Site-Directed; Protein Processing, Post-Translational/genetics; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/metabolism; Sequence Deletion |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
See also
References
See Help:References for how to manage references in EcoliWiki.