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| | !align=left |Citation | ||
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'''No author listed''' (2002) In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli. ''J. Biol. Chem.'' '''277''':48199-204 | |||
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!align=left |Abstract | |||
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The final stages of bacterial molybdenum cofactor (Moco) biosynthesis correspond to molybdenum chelation and nucleotide attachment onto an unique and ubiquitous structure, the molybdopterin. Using a bacterial two-hybrid approach, here we report on the in vivo interactions between MogA, MoeA, MobA, and MobB implicated in several distinct although linked steps in Escherichia coli. Numerous interactions among these proteins have been identified. Somewhat surprisingly, MobB, a GTPase with a yet unclear function, interacts with MogA, MoeA, and MobA. Probing the effects of various mo. mutations on the interaction map allowed us (i) to distinguish Moco-sensitive interactants from insensitive ones involving MobB and (ii) to demonstrate that molybdopterin is a key molecule triggering or facilitating MogA-MoeA and MoeA-MobA interactions. These results suggest that, in vivo, molybdenum cofactor biosynthesis occurs on protein complexes rather than by the separate action of molybdenum cofactor biosynthetic proteins. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12372836 PubMed] | |||
Online version:[http://dx.doi.org/10.1074/jbc.M205806200 10.1074/jbc.M205806200] | |||
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|{{ | !align=left |Keywords | ||
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Coenzymes; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Bacterial; Metalloproteins/biosynthesis; Metalloproteins/genetics; Molecular Probes; Mutation; Pteridines | |||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
Revision as of 18:14, 1 September 2013
| Citation |
No author listed (2002) In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli. J. Biol. Chem. 277:48199-204 |
|---|---|
| Abstract |
The final stages of bacterial molybdenum cofactor (Moco) biosynthesis correspond to molybdenum chelation and nucleotide attachment onto an unique and ubiquitous structure, the molybdopterin. Using a bacterial two-hybrid approach, here we report on the in vivo interactions between MogA, MoeA, MobA, and MobB implicated in several distinct although linked steps in Escherichia coli. Numerous interactions among these proteins have been identified. Somewhat surprisingly, MobB, a GTPase with a yet unclear function, interacts with MogA, MoeA, and MobA. Probing the effects of various mo. mutations on the interaction map allowed us (i) to distinguish Moco-sensitive interactants from insensitive ones involving MobB and (ii) to demonstrate that molybdopterin is a key molecule triggering or facilitating MogA-MoeA and MoeA-MobA interactions. These results suggest that, in vivo, molybdenum cofactor biosynthesis occurs on protein complexes rather than by the separate action of molybdenum cofactor biosynthetic proteins. |
| Links |
PubMed Online version:10.1074/jbc.M205806200 |
| Keywords |
Coenzymes; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Bacterial; Metalloproteins/biosynthesis; Metalloproteins/genetics; Molecular Probes; Mutation; Pteridines |
| edit table |
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| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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