Analysis of the<i>Escherichia coli</i>genome. III. DNA sequence of the region from 87.2 to 89.2 minutes

Plunkett, Guy; Burland, Valerie; Daniels, Donna L.; Blattner, Frederick R.

doi:10.1093/nar/21.15.3391

Cited by 149 publications

(120 citation statements)

References 55 publications

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“…The Nterminal amino acid sequence of protein C coincides with that of L31 (Wada et al 1990). But its C-terminus is eight amino acids longer than that of L31 (Brosius 1978;Plunkett et al 1993). Our recent work has shown that L31 is generated by cleavage of the primary product (C protein) with protease VII, an outer membrane protein, during the grinding or lysis of cells, since a mutant cell (AD202) disrupted in the gene for protease VII (ompT) only has proteinC.…”

Section: Introductionmentioning

confidence: 99%

Growth phase coupled modulation of Escherichia coli ribosomes

1998

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Ribosomal modulation factor (RMF), a small basic protein, expresses transcriptionally in the stationary phase of Escherichia coli cells and binds to 50S ribosomal subunits. The RMF bound 70S ribosomes dimerize to form 100S particles that have no translational activity. In transferring the stationary cells to a fresh medium, the 100S particles release the RMF and dissociate to active 70S. The interconversion of ribosomes between active 70S and inactive 100S by RMF is a cellular mechanism controlling translation.

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Section: Introductionmentioning

confidence: 99%

Growth phase coupled modulation of Escherichia coli ribosomes

1998

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“…The final step of this biosynthetic pathway requires the mob locus, which encodes functions that catalyze the synthesis of MGD from MPT and a GMP donor, most probably GTP (8). The mob locus in E. coli contains two genes, mobA and mobB, arranged as a single transcription unit (8,9). MobA is a well characterized monomeric enzyme capable of the synthesis of MGD from MPT and GMP, and it has been shown to activate the molybdoenzyme nitrate reductase (10).…”

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confidence: 99%

Insight into the Role of Escherichia coli MobB in Molybdenum Cofactor Biosynthesis Based on the High Resolution Crystal Structure

McLuskey

Harrison

Schüttelkopf

et al. 2003

Journal of Biological Chemistry

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Two proteins, which are co-transcribed in Escherichia coli (MobA and MobB), are involved in the attachment of a nucleotide moiety to the molybdenum cofactor to form active molybdopterin guanine dinucleotide. Although not essential for this process, the dimeric MobB increases the activation of molybdoenzymes, incorporating this cofactor by a mechanism that is not understood. The structure of MobB has been elucidated in two crystal forms, one of which has provided a model at 1.9-Å resolution with R work and R free values of 21.5 and 28.7%, respectively. The MobB subunit displays an ␣/␤-fold arranged into a major and minor domain, the latter of which is inserted between the major and minor domains of the partner subunit, creating an elongated dimer constructed around a 16-stranded ␤-sheet. Structural homologues have been identified, and they include a number of nucleotide-binding proteins. Comparisons indicate that although the phosphate-binding regions are highly conserved, MobB lacks the elements of structure required to interact with and efficiently bind a nucleotide base. In the present structure, a sulfate is bound to the Walker A phosphate-binding motif of MobB. The possibility that MobB forms a complex with the nucleotidebinding MobA, the protein with which it is co-transcribed, is explored, and modeling suggests that such a MobA:MobB complex is feasible. This hypothesis is supported by recent biochemical evidence indicating that MobB interacts with several proteins involved in various stages of molybdenum cofactor biosynthesis including MobA. We propose therefore that MobB is an adapter protein that acts in concert with MobA to achieve the efficient biosynthesis and utilization of molybdopterin guanine dinucleotide.Molybdenum is an essential trace element associated with a diverse range of redox-active enzymes (1). Such molybdoenzymes catalyze basic metabolic reactions in the carbon, nitrogen, and sulfur cycles exploiting the redox chemistry of this second row transition metal. With the exception of the nitrogenases that contain an iron-molybdenum-sulfur cluster, molybdenum is integrated into the enzymes as the molybdenum cofactor (Moco), 1 which contains mononuclear molybdenum coordinated to an organic cofactor termed molybdopterin (MPT).

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“…Sequence analysis of the nt-f gene product revealed sequence similarity to a 18.9-kDa protein encoded by the f170 gene located immediately downstream to the mob locus in E. coli which is also implicated with the biosynthesis of the molybdopterin cofactor (Plunkett et al, 1993).…”

Section: Resultsmentioning

confidence: 99%

The Tungsten Formylmethanofuran Dehydrogenase from Methanobacterium Thermoautotrophicum Contains Sequence Motifs Characteristic for Enzymes Containing Molybdopterin Dinucleotide

Hochheimer

Schmitz

Thauer

et al. 1995

European Journal of Biochemistry

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Formylmethanofuran dehydrogenases arc molybdenum or tungsten iron-sulfur proteins containing a pterin dinucleolide cofactor. We report here on the primary structures of the four subunits FwdABCD of the tungsten enzyme from Methmohucteriuni thermoautcltrrii~hic.unz which were dctermincd by cloning and sequencing the encoding genes jwdABCD. FwdB was found to contain sequence motifs characteristic for molybdopterin-dinucleotidc-containing cnzytncs indicating that this subunit harbors the active site. FwdA, FwdC and FwdD showed no significant sequcnce similarity lo proteins in the diila bases. Northern blot analysis revealed that the four j w d genes form a transcription unit together with three additional genes designatedfwdE,fwdF andfwdC. A 17.8-kDa protein and an 8.6-kDa protein, both containing two 14Fe-4SI cluster binding motifs, were deduced frotii f w d E and fwdC. The open reading frame ,fivdF encodes a 38.6-kDa protein containing eight binding motifs for [4Fe-4S] clusters suggesting the gene product to be a novel polyferredoxin. All seven fwtl gcnes were expresscd i n Esclwrichiu coli yielding proteins of the expecled size. Thefwd operon was found to be located in a region of the M. thernroautotruphicum genome encoding molybdenum enzymes and proteins involved i ti iiiolybdopterin hiosynthesis.Kt?ywurds: methanogenic Archaea; tungsten enzymes; molybdenum enzymes; molybdopterin; iron-sulfui proteins.Formylmethanofuran dchydrogenasc is an enzyme found in methanogenic and sulfate-reducing Archaea. It catalyzes the reversible dehydrogenation of formylmethanofuran to CO, and methanofuran (E" = -530 mV). The reaction is iiivolved in C 0 7 reduction to methane, in autotrophic CO, fixation, and i n CO, formation from reduced C, units (Bertram and Thauer, 1994;Wasserfallen, 1994; Vorholt ct al., 1995).Fortnylrnetlianofuran dehydrogenases are either molybdenum or tungsten iron-sulfur proteins. The tungsten seems to be bound to the satiic skeleton as the molybdenum in the so-callcd molybdopterin djnucleotide cofactor (Karrasch et al., 1990; Bijrner et al., 1991). In Methanobacterium wo(fei and Mr,thanobmcterium thermoaututrnphicum two isoenzymes of formylmethanofuran dehydrogenase are found, one containing molybdenum and the other tungsten (Schmitz ct al., 1992a,b; Bertram et al., 1994a,b). In M. thermoautotrophicum the active molybdenum isoenzyme is only synthesized when molybdenum is available during growth. The active tungsten enzyme is also generated during growth of the cells on molybdate medium. Under ___-Fmd, molybdenum I'ormylmcthanofuran dehydrogenase. the latter conditions the tungstcn isocnzyme is synthesized containing mvlybdenutn rather than tungsten.The tungstcn isoenzynie of M. thermooutotro/ihicum is composed of four differenl subunits of apparent niolecular masses of65 kDa (FwdA), 53 kDa (FwdB), 31 kDa (FwdC) and IS kDa (FwdD). It contains 0.4 inol tungsten, 0.6 in01 molybdopterin guanine dinucleotide and approximatcly X inol nun-heme iron and acid-labilc sulfur/mol 160-kDa native ewytiic. Thc molyb...

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Analysis of theEscherichia coligenome. III. DNA sequence of the region from 87.2 to 89.2 minutes

Cited by 149 publications

References 55 publications

Growth phase coupled modulation of Escherichia coli ribosomes

Growth phase coupled modulation of Escherichia coli ribosomes

Insight into the Role of Escherichia coli MobB in Molybdenum Cofactor Biosynthesis Based on the High Resolution Crystal Structure

The Tungsten Formylmethanofuran Dehydrogenase from Methanobacterium Thermoautotrophicum Contains Sequence Motifs Characteristic for Enzymes Containing Molybdopterin Dinucleotide

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