The High-affinity K+-translocating ATPase Complex from Clostridium acetobutylicum Consists of Six Subunits

Behrens, Martin; Schreiber, Wiebke; Dürre, Peter

doi:10.1006/anae.2001.0371

Cited by 3 publications

(4 citation statements)

References 26 publications

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“…These include Na + -ABC transporter (spot 348 b) , CAC3551), ABC transporter, ATP-binding protein (spot 398 a) , CAC0147), Oligopeptide ABC transporter, periplasmic substrate-binding component (spot 128 a) ) and several subunits (α, β, γ, δ) of ATPase (spots172 a) , 264 b) , 341 b) , 369 b) , 376 b) and 384 b) ). Except that the detection of ATPase subunits has been reported previously in C. acetobutylicum , , other membrane-associated proteins were detected for the first time in the cytoplasmic proteome of this species.…”

Section: Resultscontrasting

confidence: 42%

Proteome Reference Map and Comparative Proteomic Analysis between a Wild TypeClostridium acetobutylicumDSM 1731 and its Mutant with Enhanced Butanol Tolerance and Butanol Yield

et al. 2010

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The solventogenic bacterium Clostridium acetobutylicum is an important species of the Clostridium community. To develop a fundamental tool that is useful for biological studies of C. acetobutylicum, we established a high resolution proteome reference map for this species. We identified 1206 spots representing 564 different proteins by mass spectrometry, covering approximately 50% of major metabolic pathways. To better understand the relationship between butanol tolerance and butanol yield, we performed a comparative proteomic analysis between the wild type strain DSM 1731 and the mutant Rh8, which has higher butanol tolerance and higher butanol yield. Comparative proteomic analysis of two strains at acidogenic and solventogenic phases revealed 102 differentially expressed proteins that are mainly involved in protein folding, solvent formation, amino acid metabolism, protein synthesis, nucleotide metabolism, transport, and others. Hierarchical clustering analysis revealed that over 70% of the 102 differentially expressed proteins in mutant Rh8 were either upregulated (e.g., chaperones and solvent formation related) or downregulated (e.g., amino acid metabolism and protein synthesis related) in both acidogenic and solventogenic phase, which, respectively, are only upregulated or downregulated in solventogenic phase in the wild type strain. This suggests that Rh8 cells have evolved a mechanism to prepare themselves for butanol challenge before butanol is produced, leading to an increased butanol yield. This is the first report on the comparative proteome analysis of a mutant strain and a base strain of C. acetobutylicum. The fundamental proteomic data and analyses will be useful for further elucidating the biological mechanism of butanol tolerance and/or enhanced butanol production.

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Section: Resultscontrasting

confidence: 42%

Proteome Reference Map and Comparative Proteomic Analysis between a Wild TypeClostridium acetobutylicumDSM 1731 and its Mutant with Enhanced Butanol Tolerance and Butanol Yield

et al. 2010

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“…The KdpZ, KdpY and KdpX are also shown to be a part of the functional Kdp complex from C. acetobutylicum. (Behrens et al 2001). In Mycobacterium tuberculosis, the arrangement (Walderhaug et al 1992, Gassel et al 1999, Anabaena L-31 kdp1/kdp2 , Anabaena 7120 kdp1/ kdp2 (Kaneko et al 2001), Synechocystis 6803 (Kaneko et al 1996), Deinococcus radiodurans kdp (White et al 1999), Clostridium acetobutylicum kdp (Treuner-Lange et al 1997), Mycobacterium tuberculosis kdp (Cole et al 1998), Alicyclobacillus acidocaldarius kdp (Schleussinger et al 2006).…”

Section: Organization Of Kdp Operons In Bacteriamentioning

confidence: 99%

The Kdp-ATPase system and its regulation

2007

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K+, the dominant intracellular cation, is required for various physiological processes like turgor homeostasis, pH regulation etc. Bacterial cells have evolved many diverse K+ transporters to maintain the desired concentration of internal K+. In E.coli, the KdpATPase (comprising of the KdpFABC complex), encoded by the kdpFABC operon, is an inducible high-affinity K+ transporter that is synthesised under conditions of severe K+ limitation or osmotic upshift. The E.coli kdp expression is transcriptionally regulated by the KdpD and KdpE proteins, which together constitute a typical bacterial two-component signal transduction system. The Kdp system is widely dispersed among the different classes of bacteria including the cyanobacteria. The ordering of the kdpA, kdpB and kdpC is relatively fixed but the kdpD/E genes show different arrangements in distantly related bacteria. Our studies have shown that the cyanobacterium Anabaena sp. strain L-31 possesses two kdp operons, kdp1 and kdp2, of which, the later is expressed under K+ deficiency and desiccation. Among the regulatory genes,the kdpD ORF of Anabaena L-31 is truncated when compared to the kdpD of other bacteria, while a kdpE -like gene is absent. The extremely radio-resistant bacterium, Deinococcus radiodurans strain R1, also shows the presence of a naturally short kdpD ORF similar to Anabaena in its kdp operon. The review elaborates the expression of bacterial kdp operons in response to various environmental stress conditions, with special emphasis on Anabaena. The possible mechanism(s)of regulation of the unique kdp operons from Anabaena and Deinococcus are also discussed.

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“…strain L-31 kdpG appeared to encode a hydrophobic protein with two transmembrane segments. The KdpG, which is unique to cyanobacterial genomes, may play a role in stabilization or activity of the KdpATPase complex, as has been shown for KdpF and KdpY-Z in other organisms (10,17). A naturally short kdpD ORF was observed downstream of kdpC1, while no such ORF was observed in the kdp2 operon of Anabaena sp.…”

Section: Resultsmentioning

confidence: 72%

“…strain L-31 kdp operons showed very good homology to other bacterial KdpABC proteins (Table 1). Many kdp operons from other bacteria show the presence of small ORFs encoding for hydrophobic peptides, e.g., kdpF in E. coli (17) and M. tuberculosis (14) and kdpZ and kdpY in C. acetobutylicum (10). Although a kdpF-like gene was absent from the two Anabaena sp.…”

Section: Resultsmentioning

confidence: 99%

Differential Expression of the Two kdp Operons in the Nitrogen-Fixing Cyanobacterium Anabaena sp. Strain L-31

Ballal

Apte

2005

Appl Environ Microbiol

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In several types of bacteria, the Kdp ATPase (comprising of the KdpABC complex) is an inducible, high-affinity potassium transporter that scavenges K ؉ from the environment. The cyanobacterium Anabaena sp. strain L-31 showed the presence of not one but two distinct kdp operons in its genome. The kdp1 consisted of kdpA1B1G1C1D genes, whereas the kdp2 contained the kdpA2B2G2C2 genes. Among the regulatory genes, the kdpD open reading frame of Anabaena sp. strain L-31 was truncated compared to the kdpD of other bacteria, whereas a kdpE-like gene was absent in the vicinity of the two kdp operons. In response to K ؉ limitation (<0.05 mM external K ؉ ), only kdp2 (and not kdp1) expression could be detected as a 5.3-kb transcript on Northern blots, indicating that kdpA2B2G2C2 genes constitute a polycystronic operon. Unlike E. coli, addition of osmolytes like NaCl, or a change in pH of the medium did not enhance the kdp expression in Anabaena sp. strain L-31. Interestingly, the Anabaena sp. strain L-31 kdp2 operon was strongly induced in response to desiccation stress. The addition of K ؉ to K ؉ -starved cultures resulted in repression and degradation of kdp2 transcripts. Our results clearly show that kdp2 is the major kdp operon expressed in Anabaena sp. strain L-31 and may play an important role in adaptation to K ؉ limitation and desiccation stress.Potassium, the major intracellular cation in bacteria, is involved in various physiological processes such as turgor adaptation (15), activation of cellular enzymes (29), and pH homeostasis (12). In nitrogen-fixing cyanobacteria such as Anabaena spp., K ϩ also regulates gene expression and vital metabolic processes such as photosynthesis and nitrogen fixation (1, 2). Despite very low levels of K ϩ available in most environments (0.1 to 10 mM), the bacteria maintain a very high concentration of K ϩ (0.2 to 0.6 M) within their cells and have evolved several distinct K ϩ uptake and efflux systems to regulate their internal K ϩ concentration (15). In Escherichia coli the constitutively expressed TrkG, TrkH, and Kup uptake systems have a low affinity for K ϩ but are competent to maintain the required levels K ϩ under normal physiological conditions (20). Under conditions of severe K ϩ limitation or osmotic upshift or when the low-affinity transporters are unable to meet the cell's demand for K ϩ , the high-affinity KdpATPase (K ϩ -dependent ATPase) is expressed (4). The K m of E. coli KdpATPase for K ϩ is 2 M and the cells expressing Kdp can reduce the K ϩ concentration in the medium to as low as 50 nM (28).Earlier studies had shown the kdp homologs to be widely distributed among the gram-negative bacteria (32). Genome sequencing has now shown kdp homologs to be present also in cyanobacteria, gram-positive bacteria, and the Archaea. We have previously demonstrated the presence of KdpB-like polypeptide in three different strains of the nitrogen-fixing cyanobacteria Anabaena spp. (6). The KdpB was induced under conditions of K ϩ limitation, and the KdpB protein was shown to be loc...

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The High-affinity K+-translocating ATPase Complex from Clostridium acetobutylicum Consists of Six Subunits

Cited by 3 publications

References 26 publications

Proteome Reference Map and Comparative Proteomic Analysis between a Wild TypeClostridium acetobutylicumDSM 1731 and its Mutant with Enhanced Butanol Tolerance and Butanol Yield

Proteome Reference Map and Comparative Proteomic Analysis between a Wild TypeClostridium acetobutylicumDSM 1731 and its Mutant with Enhanced Butanol Tolerance and Butanol Yield

The Kdp-ATPase system and its regulation

Differential Expression of the Two kdp Operons in the Nitrogen-Fixing Cyanobacterium Anabaena sp. Strain L-31

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