The F1FOATP synthase genes inMethanosarcina acetivoransare dispensable for growth and ATP synthesis

Saum, Regina; Schlegel, Katharina; Meyer, Benjamin; Müller, Volker

doi:10.1111/j.1574-6968.2009.01785.x

Cited by 18 publications

(19 citation statements)

References 25 publications

(33 reference statements)

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“…S6). This showed that N-ATPase contains at least part of the δ-subunit, in agreement with the earlier analyses (Saum et al , 2009). …”

Section: Resultssupporting

confidence: 93%

“…S1). As has been noted previously (Meier et al , 2009; Saum et al , 2009), this Glu residue could potentially provide two ligands for the Na + ion and thereby complete the Na + coordination shell. If so, all these N-ATPases would end up being capable of binding Na + ions.…”

Section: Discussionsupporting

confidence: 62%

“…Although this gene was originally marked as atpI (Sumi et al , 1997) and is occasionally still labeled this way (Saum et al , 2009), its product shows no statistically significant sequence similarity to the genuine AtpI (UncI) proteins, previously described in the genomes of Escherichia coli and other model organisms. In accordance with their distinct sequences, AtpI and AtpQ proteins are assigned to two different Pfam families, PF03899 and PF09527, respectively, and to two different COGs, COG3312 and COG5536 in the CDD database (Marchler-Bauer et al , 2009).…”

Section: Resultsmentioning

confidence: 99%

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Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase

2010

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An analysis of the distribution of the Na+-translocating ATPases/ATP synthases among microbial genomes identified an atypical form of the F1Fo-type ATPase that is present in the archaea Methanosarcina barkeri and M.acetivorans, in a number of phylogenetically diverse marine and halotolerant bacteria and in pathogens Burkholderia spp. In complete genomes, representatives of this form (referred to here as N-ATPase) are always present as second copies, in addition to the typical proton-translocating ATP synthases. The N-ATPase is encoded by a highly conserved atpDCQRBEFAG operon and its subunits cluster separately from the equivalent subunits of the typical F-type ATPases. N-ATPase c subunits carry a full set of sodium-binding residues, indicating that most of these enzymes are Na+-translocating ATPases that likely confer on their hosts the ability to extrude Na+ ions. Other distinctive properties of the N-ATPase operons include the absence of the delta subunit from its cytoplasmic sector and the presence of two additional membrane subunits, AtpQ (formerly gene 1) and AtpR (formerly gene X). We argue that N-ATPases are an early-diverging branch of membrane ATPases that, similarly to the eukaryotic V-type ATPases, do not synthesize ATP.Contact: galperin@ncbi.nlm.nih.gov; amulkid@uos.deSupplementary information: Supplementary data are available at Bioinformatics online.

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“…S6). This showed that N-ATPase contains at least part of the δ-subunit, in agreement with the earlier analyses (Saum et al , 2009). …”

Section: Resultssupporting

confidence: 93%

Section: Discussionsupporting

confidence: 62%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase

2010

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“…Although it is conceivable that the atp -type genes may be significantly expressed under unknown growth conditions, an alternative possibility is that they constitute a "dead-ended" lateral gene transfer event [23]. Interestingly, the deletion of the atp gene region of M. acetivorans conferred no phenotype [25]. The atpX gene present in the M. acetivorans and M. barkeri genomes is conserved in some, but not all bacterial-like ATP synthase operons.…”

Section: Discussionmentioning

confidence: 99%

Carbon-dependent control of electron transfer and central carbon pathway genes for methane biosynthesis in the Archaean, Methanosarcina acetivorans strain C2A

Rohlin

Gunsalus

2010

BMC Microbiol

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BackgroundThe archaeon, Methanosarcina acetivorans strain C2A forms methane, a potent greenhouse gas, from a variety of one-carbon substrates and acetate. Whereas the biochemical pathways leading to methane formation are well understood, little is known about the expression of the many of the genes that encode proteins needed for carbon flow, electron transfer and/or energy conservation. Quantitative transcript analysis was performed on twenty gene clusters encompassing over one hundred genes in M. acetivorans that encode enzymes/proteins with known or potential roles in substrate conversion to methane.ResultsThe expression of many seemingly "redundant" genes/gene clusters establish substrate dependent control of approximately seventy genes for methane production by the pathways for methanol and acetate utilization. These include genes for soluble-type and membrane-type heterodisulfide reductases (hdr), hydrogenases including genes for a vht-type F420 non-reducing hydrogenase, molybdenum-type (fmd) as well as tungsten-type (fwd) formylmethanofuran dehydrogenases, genes for rnf and mrp-type electron transfer complexes, for acetate uptake, plus multiple genes for aha- and atp-type ATP synthesis complexes. Analysis of promoters for seven gene clusters reveal UTR leaders of 51-137 nucleotides in length, raising the possibility of both transcriptional and translational levels of control.ConclusionsThe above findings establish the differential and coordinated expression of two major gene families in M. acetivorans in response to carbon/energy supply. Furthermore, the quantitative mRNA measurements demonstrate the dynamic range for modulating transcript abundance. Since many of these gene clusters in M. acetivorans are also present in other Methanosarcina species including M. mazei, and in M. barkeri, these findings provide a basis for predicting related control in these environmentally significant methanogens.

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“…One notable exception is Methanosarcina acetivorans, which has genes for both F-type and A-type ATP synthases. Saum et al (56) have recently shown that the F-type ATP synthase is not essential for the growth of M. acetivorans. The M. ruminantium M1 genome contains an ahaHIKECFABD operon, and no genes for an F-type enzyme were identified.…”

Section: Discussionmentioning

confidence: 99%

A1Ao-ATP Synthase of Methanobrevibacter ruminantium Couples Sodium Ions for ATP Synthesis under Physiological Conditions

McMillan

Ferguson

Dey

et al. 2011

Journal of Biological Chemistry

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Background: An enigma in the bioenergetics of methanogens is how the generation of proton and sodium gradients are used to synthesize ATP. Results: Purified methanogen ATP synthase was stimulated by sodium ions that also provided pH-dependent protection against DCCD. Conclusion:Methanobrevibacter ruminantium harbors an A-type enzyme with the ability to switch between sodium ions and protons. Significance: ATP synthesis by methanogens depends on the environmental conditions that prevail.

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The F₁F_OATP synthase genes inMethanosarcina acetivoransare dispensable for growth and ATP synthesis

Cited by 18 publications

References 25 publications

Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase

Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase

Carbon-dependent control of electron transfer and central carbon pathway genes for methane biosynthesis in the Archaean, Methanosarcina acetivorans strain C2A

A1Ao-ATP Synthase of Methanobrevibacter ruminantium Couples Sodium Ions for ATP Synthesis under Physiological Conditions

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