The complete amino acid sequence confirms the presence of pseudoazurin in <i>Thiosphaera pantotropha</i>

Chan, Christopher; Willis, Anthony C.; Robinson, Carol V.; Aplin, Robin T.; Radford, Sheena E.; Ferguson, Stuart J.

doi:10.1042/bj3080585

Cited by 11 publications

(12 citation statements)

References 25 publications

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“…In cytochrome c, electrospray of the protein unfolded in either acid (12) or at high temperature (13) results in a charge distribution that is broader and centered on a much higher charge than when the protein is sprayed from its native state. Similar observations have been made for a number of proteins in our laboratory including lysozyme, a-lactalbumin, GroEL, and pseudoazunn (14). This phenomenon may be attributed, in part, to the lower free energy of distributing like charges disparately on extended rather than compact structures (12, 15).…”

Section: Rules Governing Proteinsupporting

confidence: 79%

Investigation of protein folding by mass spectrometry

et al. 1996

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Mass spectrometry is emerging as one of the most exciting new techniques being applied to studies of protein folding. Recent developments in soft ionization techniques enable intact proteins to be generated in the gas phase from aqueous solution, and fragmentation methods are providing a means of obtaining sequence-specific information. These techniques, particularly in combination with established methods such as NMR spectroscopy, allow the investigation of both covalent and noncovalent events that occur during refolding processes. One important type of application involves mass spectrometry in an analytical role, for example, in characterizing the products of oxidative refolding experiments. Mass spectrometry can also be used to reveal fundamentally new information about the conformational properties of folding intermediates, both in isolation and in complexes with molecular chaperones, through the exploitation of hydrogen-deuterium exchange phenomena. Of particular interest is the insight this approach can provide into the cooperativity of structure formation and the distribution of intermediates at different steps along folding pathways. In this paper we describe recent insights into protein folding resulting from the application of mass spectrometry and discuss the future potential of the method for studies in this area.

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Section: Rules Governing Proteinsupporting

confidence: 79%

Investigation of protein folding by mass spectrometry

et al. 1996

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“…These gene and protein sequences are very similar to their counterparts in the closely related organism (37) Paracoccus pantotrophus (11,25). However, immediately beyond the structural gene region the DNA sequences of P. pantotrophus and P. denitrificans had considerable differences.…”

Section: Resultsmentioning

confidence: 54%

A Mutant of Paracoccus denitrificans with Disrupted Genes Coding for Cytochrome c ₅₅₀ and Pseudoazurin Establishes These Two Proteins as the In Vivo Electron Donors to Cytochrome cd ₁ Nitrite Reductase

et al. 2003

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In Paracoccus denitrificans, electrons pass from the membrane-bound cytochrome bc 1 complex to the periplasmic nitrite reductase, cytochrome cd 1 . The periplasmic protein cytochrome c 550 has often been implicated in this electron transfer, but its absence, as a consequence of mutation, has previously been shown to result in almost no attenuation in the ability of the nitrite reductase to function in intact cells. Here, the hypothesis that cytochrome c 550 and pseudoazurin are alternative electron carriers from the cytochrome bc 1 complex to the nitrite reductase was tested by construction of mutants of P. denitrificans that are deficient in either pseudoazurin or both pseudoazurin and cytochrome c 550 . The latter organism, but not the former (which is almost indistinguishable in this respect from the wild type), grows poorly under anaerobic conditions with nitrate as an added electron acceptor and accumulates nitrite in the medium. Growth under aerobic conditions with either succinate or methanol as the carbon source is not significantly affected in mutants lacking either pseudoazurin or cytochrome c 550 or both these proteins. We concluded that pseudoazurin and cytochrome c 550 are the alternative electron mediator proteins between the cytochrome bc 1 complex and the cytochrome cd 1 -type nitrite reductase. We also concluded that expression of pseudoazurin is mainly controlled by the transcriptional activator FnrP.

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“…The nodules formed by this mutant (VF39-TP5) were indistinguishable from those of the wild-type strain, and acetylene reduction assays revealed nitrogenase activities of approx. 75% (Ambler and Tobari, 1985), Vibrio alginolyticus (Va) (Petratos et al, 1987), A. faecalis (Af) (Yamamoto et al, 1987) and Thiosphaera pantotropha (Tp) (Chan et al, 1995). Amino acid residues identical in all four sequences are marked by asterisks.…”

Section: Figmentioning

confidence: 99%

Rhizobium leguminosarum bv. viciae contains a second fnr/fixK‐like gene and an unusual fixL homologue

Patschkowski

Schlüter

Priefer

1996

Molecular Microbiology

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Genes of Rhizobium leguminosarum bv. viciae VF39 coding for the regulatory elements NifA, FixL and FixK were isolated, sequenced and genetically analysed. The fixK-fixL region is located upstream of the fixNOQP operon on the non-nodulation plasmid pRleVF39c. The deduced amino acid sequence of FixL revealed an unusual structure in that it contains a receiver module (homologous to the N-terminal domain of response regulators) fused to its transmitter domain. An oxygen-sensing haem-binding domain, found in other FixL proteins, is conserved in R, leguminosarum bv. viciae FixL. R. leguminosarum bv. viciae possesses a second fnr-like gene, designated fixK, whose encoded gene product is very similar to Rhizobium meliloti and Azorhizobium caulinodans FixK. Individual R. leguminosarum bv. viciae fixK and fixL insertion mutants displayed a Fix+ phenotype. A reduced nitrogen-fixation activity was found for a R. leguminosarum bv. viciae fnrN-deletion mutant, whereas no nitrogen-fixation activity was detectable for a flxK/fnrN double mutant. The R. leguminosarum bv. viciae nifA gene is expressed independently of FixL and FixK under aerobic and microaerobic conditions, whereas fixL gene expression is induced under microaerobiosis. Another orf was identified down-stream of fixK-fixL and encodes a product which has homology to pseudoazurins from different species. Mutation of this azu gene showed that it is dispensable for nitrogen fixation.

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The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha

Cited by 11 publications

References 25 publications

Investigation of protein folding by mass spectrometry

Investigation of protein folding by mass spectrometry

A Mutant of Paracoccus denitrificans with Disrupted Genes Coding for Cytochrome c ₅₅₀ and Pseudoazurin Establishes These Two Proteins as the In Vivo Electron Donors to Cytochrome cd ₁ Nitrite Reductase

Rhizobium leguminosarum bv. viciae contains a second fnr/fixK‐like gene and an unusual fixL homologue

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The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha

Cited by 11 publications

References 25 publications

Investigation of protein folding by mass spectrometry

Investigation of protein folding by mass spectrometry

A Mutant of Paracoccus denitrificans with Disrupted Genes Coding for Cytochrome c 550 and Pseudoazurin Establishes These Two Proteins as the In Vivo Electron Donors to Cytochrome cd 1 Nitrite Reductase

Rhizobium leguminosarum bv. viciae contains a second fnr/fixK‐like gene and an unusual fixL homologue

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A Mutant of Paracoccus denitrificans with Disrupted Genes Coding for Cytochrome c ₅₅₀ and Pseudoazurin Establishes These Two Proteins as the In Vivo Electron Donors to Cytochrome cd ₁ Nitrite Reductase