PMID:12372836: Difference between revisions

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<span style = 'font-size: large'> '''Magalon, A, Frixon, C, Pommier, J, Giordano, G and Blasco, F'''  (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</span>
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|{{TableHeadingColor}} |'''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.
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'''Magalon, A, Frixon, C, Pommier, J, Giordano, G and Blasco, F'''  (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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[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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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12372836 PubMed]
!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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Latest revision as of 04:18, 15 September 2013

Citation

Magalon, A, Frixon, C, Pommier, J, Giordano, G and Blasco, F (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

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