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PubMed1996

Solution X-ray scattering data show structural differences between yeast and vertebrate calmodulin: implications for structure/function.

We present here the first evidence, obtained by the use of solution X-ray scattering, of the solution structure of yeast calmodulin, a poor activator of vertebrate enzymes. The radius of gyration of yeast calmodulin decreased from 21.1 to 19.9 angstroms when excess Ca2+ ions were added. The profiles of the pair-distribution function suggested that yeast calmodulin without Ca2+ has a dumbbell-like shape which changes toward a rather asymmetric globular shape, from its dumbbell shape, by the binding of Ca2+. In the presence of a calmodulin binding peptide such as MLCK-22 (a synthetic peptide corresponding to residues 577-598 of skeletal myosin light chain kinase), the radius of gyration of yeast calmodulin decreased by 1.6 angstroms, and the molecular shape of it estimated from the profile of the pair-distribution function was globular but less compact than that of vertebrate calmodulin. These results for the structure of yeast calmodulin complexed with Ca2+ and with Ca(2+)-peptides are quite different from those of vertebrate calmodulin. Thus, the functional differences between yeast and vertebrate calmodulin which we reported previously [Matsuura, I., et al. (1993) J. Biol. Chem. 268, 13267-13273] have been interpreted on the basis of the structural differences between them. Moreover, the structural studies on chimeric proteins of chicken and yeast calmodulin suggest that Ca2+ binding at site IV is essential to form the full active dumbbell structure, which is characteristic of vertebrate-type calmodulin.

Amino Acid Sequence↗
PubMed1999

Calcium binding induces interaction between the N- and C-terminal domains of yeast calmodulin and modulates its overall conformation.

Calmodulin from the yeast Saccharomyces cerevisiae binds 3 mol of Ca2+ cooperatively. We report here lines of evidence supporting the intramolecular interaction between the N- and C-terminal domains which modulates the Ca2+ binding properties of yeast calmodulin. First, the sum of the Ca2+ binding curves of the N-terminal and the C-terminal half-molecule did not yield the Ca2+ binding curve of yeast calmodulin. Second, the mean residue CD of yeast calmodulin at 222 nm (-Delta epsilon222) decreased with increases in the concentration of Ca2+, whereas those of each half-molecule increased. Finally, the C2 proton of His107 in the C-terminal domain of yeast calmodulin showed three resonance peaks with increases in the concentration of Ca2+, each corresponding to the apo, the intermediate, and the Ca2+-saturated state. The intermediate peak could not be observed in the C-terminal half-molecule of yeast calmodulin. Computer simulation considering the macroscopic Ca2+ binding constants assigned this intermediate to a species consisting of the apo C-terminal domain and the N-terminal domain with at least one of the two sites occupied by Ca2+. Peptide segments spanning the defective fourth Ca2+ binding site may be involved in the interdomain interaction and the yeast-specific function of calmodulin.

Binding Sites↗
PubMed1999

Effects of added yeast on protein transmission and flux in cross-flow membrane microfiltration

Microfiltration membranes may be used to separate valuable proteins from suspensions containing cells or cell debris. Although a clean microfiltration membrane allows for complete protein transmission and high flux, both of these quantities decline in time due to membrane fouling. Using bovine serum albumin (BSA) as a model protein, flux and protein transmission during cross-flow microfiltration were studied with and without added yeast cells. Cross-flow microfiltration of BSA-only solutions results in a BSA fouling layer with low permeability forming on the membrane surface. Due to this layer, the long-term BSA transmission is typically only 25-40%. In contrast, during microfiltration of yeast-BSA mixtures, the yeast forms a cake layer on the membrane surface. The yeast cake acts as a dynamic or secondary membrane, allowing BSA monomers to pass through but preventing protein aggregates from fouling the membrane. The result is slower flux decline and higher long-term BSA transmission of typically 60-90%. For filtration of yeast-BSA mixtures at low yeast concentrations (<1 g/L), 50-100% higher BSA recovery is obtained than for BSA-only solutions with the same BSA concentration. At high yeast concentrations (>5 g/L), the protein transmission remains high, but the recovery may be lower due to reduced flux.

Journal Article↗
PubMed2001

Definitive evidence for the actual contribution of yeast in the transformation of neutral precursors of grape aromas.

Experiments were designed to demonstrate the actual contribution of yeast in the formation of the primary aroma during the vinification of neutral grapes. Ruché was chosen as the model wine to study because of its unique fragrance. A yeast strain specific for Ruché was selected using a new and rapid isolation method for red wines. The results of this study can be summarized as follows: Skins from nonaromatic white or red grapes apparently contain most of the primary aroma compounds that are revealed in the must only after contact with yeast cells under defined conditions. Similar results were obtained with the pulp and seeds fractions; however, the olfactory notes, although well characterized, differed from those obtained with skins alone. Clarification, filtration, and centrifugation of the pulp and seed fractions or sonification of the skins produce different and well-characterized olfaction notes during the contact with yeast. The primary aroma of nonaromatic white and red grapes contained in the skins can be revealed within 24-48 h of yeast contact in a synthetic nutrient medium (SNM). The primary aroma precursors extracted from the skins with methanol, water-saturated butanol, or aqueous buffer at pH 3.2, concentrated and eluted from a C18 resin column, can be transformed to the free form wine aroma markers within 6 h of contact with yeast cells in SNM. By contrast, prolonged maceration of the skins in aqueous alcoholic buffer at pH 3.2 or 1.1, at 50 or 70 degrees C did not release primary odors typical of wine. The individual primary aroma compounds, identified by GC-MS analysis in Ruché wine samples or in Ruché skin-yeast-SNM samples, could not explain the complexity of the typical Ruché wine odor. Only odors common to many wine varieties were identified by GC-olfactometry analysis.

Fruit↗
PubMed2002

Immobilization of yeast cells with polymeric carrier cross-linked using radiation technique.

Various compositions of 2-hydroxyethacrylate (HEA) and methoxy polyethylene glycol methacrylate (M23G) monomers were irradiated by gamma-rays at low temperature (-78 degrees C) to synthesize polymer carriers for effectively immobilizing yeast cells. The yeast cells were immobilized by cell adhesion onto/in these polymers. The ethanol productivity of immobilized yeast cells with the polymer carriers was higher than that of free cells, increasing by 1-3 times. However, the ethanol productivity of immobilized yeast with the polymer carrier resulting from 7%/7% (HEA/M23G) monomer was low, comparatively. The effect of adding cross-linking reagent (4G) to the low concentration of HEA/M23G monomers on the activity of yeast cells immobilized with the cross-linked carriers by radiation polymerization was investigated. The ethanol productivity of immobilized cells with the carriers, which were cross-linked by adding 3-6% 4G to the low concentration of HEA/M23G monomer, was increased by 20-30%, because the pore size, network structure, and mechanical strength of the polymer carriers was well adjusted and cell leakage from the polymer carriers decreased. The relationship between the ethanol productivity of immobilized yeast cells and the interior structure of polymer carriers is discussed and indicated that the interior structure of polymer carriers is crucial for effective immobilization of yeast cells.

Acrylates↗
PubMed1999

Synchronization of yeast cell populations.

The study of synchronous populations of yeast cells has provided a wealth of information into regulatory aspects of the eukaryotic cell division cycle. Synchronized yeast cultures may also have potential benefit when exploiting yeasts in biotechnology. This paper provides an overview of the methods which have been used in the synchronization of cell division in budding and fission yeasts. The relative merits of these methods are outlined and protocols for preferred synchronization methods, based on size selection techniques, are described. In particular, centrifugal elutriation protocols for Saccharomyces cerevisiae (budding yeast) and Schizosaccharomyces pombe (fission yeast) are detailed as this method is regarded as one of the best ways of preparing 'unperturbed' synchronous yeast cultures for cell cycle studies.

Cell Cycle↗
PubMedDate not supplied

Expression of a bacterial modification methylase gene in yeast.

Methylation of specific cytosines in the DNA is generally believed to play some role in the regulation of gene expression in eukaryotes. However, some eukaryotes, such as Drosophila and yeast (S. Hattman, personal communication) seem not to contain 5-methylcytosine in their DNA. It would be interesting to test, how gene expression in such organisms would respond to the methylation of specific cytosines in the genome. As a first step towards this goal, we have introduced the gene encoding the Bacillus sphaericus R modification methylase, which methylates the internal cytosine within the recognition sequence 5'-GGCC, into yeast cells. Southern-type hybridization to DNAs isolated from the transformed yeast clones revealed that the yeast plasmid carrying the prokaryotic methylase gene, as well as the two chromosomal genes tested (his3 and leu2) were methylated, whereas the bulk of the yeast DNA remained largely unmethylated. This indicates that the Bacillus sphaericus modification methylase was expressed in yeast but it modified only certain parts of the yeast DNA.

Bacillus↗
PubMed1997

Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage.

We report the cloning of a human homolog of the yeast OGGC1 gene, which encodes a DNA glycosylase that excises an oxidatively damaged form of guanine, 8-hydroxyguanine (also known as 7,8-dihydro-8-oxoguanine). Since the deduced amino acid sequence (68 amino acids) of a human expressed sequence tag, N55394, matched a short stretch of yeast OGG1 protein with greater than 40% amino acid identity, a full length cDNA clone was isolated from a HeLa cell cDNA library with the N55394 clone as a probe. The cDNA clone encodes a predicted protein of 345 amino acids which is homologous to yeast OGG1 protein throughout the entire polypeptide sequence and shares 38% amino acid identity with yeast OGG1 protein. Moreover, we found that both a human homolog and yeast OGG1 protein possess two distinct DNA binding motifs, a helix-hairpin-helix (HhH) motif and a C2H2 zinc finger like motif, and a domain homologous to human and E. coli MutY proteins. Expression of a human homolog suppressed spontaneous mutagenesis of an E. coli (mutM mutY) mutant as in the case of yeast OGG1 protein. The gene was ubiquitously expressed in a variety of human organs and mapped to chromosome 3p26.2. These results strongly suggest that the gene isolated here is a human counterpart of the yeast OGGI gene and is involved in the repair of oxidative DNA damage in human cells.

Amino Acid Sequence↗
PubMed2005

Mycosporines from freshwater yeasts: a trophic cul-de-sac?

Mycosporine-like amino-acids (MAAs) are found in aquatic bacteria, algae, and animals. A related compound, the mycosporine-glutaminol-glucoside (myc-glu-glu), has recently been reported in freshwater yeasts. Although animals depend on other organisms as their source of MAAs, they can efficiently accumulate them in their tissues. In this work we assessed the potential transfer of the yeast mycosporine myc-glu-glu from the diet into the copepod Boeckella antiqua and the ciliate Paramecium bursaria. For this purpose, we performed experiments to study the feeding of B. antiqua and P. bursaria on the yeast Rhodotorula minuta and their ability to bioaccumulate myc-glu-glu. Bioaccumulation of myc-glu-glu in B. antiqua was assessed through long-term factorial experiments manipulating the diet (Chlamydomonas reinhardii and C. reinhardii + yeasts) and radiation exposure (PAR and PAR + UVR). Shorter term experiments were designed in the case of P. bursaria. The composition and concentration of MAAs in the diet and in the consumers were determined by HPLC analyses. Our results showed that even though both consumers ingested yeast cells, they were unable to accumulate myc-glu-glu. Moreover, when exposed to conditions that stimulated the accumulation of photoprotective compounds (i.e. UVR exposure), an increase in MAAs concentration occurred in copepods fed C. reinhardii plus yeasts as well as in those fed only C. reinhardii. This suggests that the copepods were able to modify their tissue concentrations of MAAs in response to environmental clues but also that the contribution of yeast mycosporines to total MAAs concentration was negligible.

Animal Nutritional Physiological Phenomena↗
PubMed2001

A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast.

Uncoupling protein 1 (UCP1) from mouse was expressed in yeast and the specific (GDP-inhibitable) and artifactual (GDP-insensitive) effects on mitochondrial uncoupling were assessed. UCP1 provides a GDP-inhibitable model system to help interpret the uncoupling effects of high expression in yeast of other members of the mitochondrial carrier protein family, such as the UCP1 homologues UCP2 and UCP3. Yeast expressing UCP1 at modest levels (approx. 1 microg/mg of mitochondrial protein) showed no growth defect, normal rates of chemically uncoupled respiration and an increased non-phosphorylating proton conductance that was completely GDP-sensitive. The catalytic-centre activity of UCP1 in these yeast mitochondria was similar to that in mammalian brown-adipose-tissue mitochondria. However, yeast expressing UCP1 at higher levels (approx. 11 microg/mg of mitochondrial protein) showed a growth defect. Their mitochondria had depressed chemically uncoupled respiration rates and an increased proton conductance that was partly GDP-insensitive. Thus, although UCP1 shows native behaviour at modest levels of expression in yeast, higher levels (or rates) of expression can lead to an uncoupling that is not a physiological property of the native protein and is therefore artifactual. This observation might be important in the interpretation of results from experiments in which the functions of UCP1 homologues are verified by their ability to uncouple yeast mitochondria.

Animals↗
PubMed1976

Some properties of an alcohol dehydrogenase partially purified from baker's yeast grown without added zinc.

Alcohol dehydrogenase was partially purified from yeast (Saccharomyces cerevisiae) grown in the presence of 20 muM-MnSO4 without added Zn2+ and from yeast grown in the presence of 1.8 muM-MnSO4. The enzyme from yeast grown with added Zn2+ has the same properties as the crystalline enzyme from commercial supplies of baker's yeast. The enzyme from yeast grown without added An2+ has quite different properties. It has a mol.wt. in the region of 72000 and an S 20 w of 5.8S. The values can be compared with a mol.wt. of 141000 and an S 20 w of 7.6S for the crystalline enzyme. ADP-ribose, a common impurity in commercial samples of NAD+, is a potent competitive inhibitor of the new enzyme (K1 = 0.5 muM), but is not so for the crystalline enzyme. The observed maximum rate of ethanol oxidation at pH 7.05 and 25 degrees C was decreased 12-fold by the presence of 0.06 mol of inhibitor/mol of NAD+ when using the enzyme from Zn2+-deficient yeast, but with crystalline enzyme the maximum rate was essentially unchanged by this concentration of inhibitor. The kinetic characteristics for the two enzymes with ethanol, butan-1-ol, acetaldehyde and butyraldehyde as substrates are markedly different. These kinetic differences are discussed in relation to the mechanism of catalysis for the enzyme from Zn2+-deficient yeast.

Acetaldehyde↗
PubMed2002

Expression and regulation of the AMP-activated protein kinase-SNF1 (sucrose non-fermenting 1) kinase complexes in yeast and mammalian cells: studies using chimaeric catalytic subunits.

Mammalian AMP-activated protein kinase (AMPK) and yeast SNF1 (sucrose non-fermenting 1) kinase are members of a highly conserved protein kinase family that plays an important role in energy homoeostasis. AMPK and SNF1 kinase are heterotrimeric complexes consisting of a catalytic subunit and two regulatory subunits. We swapped the C-terminal regulatory domains of the catalytic subunits of AMPK (alpha) and SNF1 kinase (Snf1) and compared the expression and regulation of these chimaeric proteins with the native catalytic subunits in both mammalian and yeast cells. In mammalian cells, alpha1-Snf1 yielded a functional kinase complex following co-expression with the yeast regulatory subunits Sip2 and Snf4. Unlike native AMPK, the alpha 1-Snf1 complex was not activated by the stresses that deplete intracellular AMP. Significantly, hyperosmotic stress led to the marked activation of both the alpha 1-Snf1 complex and AMPK, without a detectable change in adenine nucleotide levels, indicating that an alternative, non-AMP-dependent, pathway was responsible for activation. alpha1-Snf1 was able to restore growth of snf1 mutant yeast on raffinose and phosphorylated the transcriptional repressor protein Mig1. Co-expression of the AMPK trimeric complex in yeast yielded an activity, increased by low glucose, that was similar to native SNF1 kinase. Importantly, expression of AMPK restored growth of a snf1 mutant on raffinose. Our results provide clues to the regulation of AMPK and SNF1 kinase and demonstrate that, in mammalian cells, there are at least two pathways that can activate AMPK, namely one that involves an increase in the AMP/ATP ratio and one that is independent of this ratio. In yeast, the glucose signalling pathway is able to activate AMPK, suggesting that the mammalian and yeast kinase pathways are conserved.

AMP-Activated Protein Kinase Kinases↗
PubMed1998

Different susceptibilities of yeasts and conidia of Penicillium marneffei to nitric oxide (NO)-mediated fungicidal activity of murine macrophages.

Penicillium marneffei is an important opportunistic fungal pathogen. Host defence mechanisms against P. marneffei are not fully understood. We investigated the fungicidal activity of murine peritoneal macrophages against two forms of P. marneffei, conidia and yeast cells, and the involvement of the NO-mediated killing system. Peritoneal macrophages suppressed the intracellular growth of P. marneffei yeast cells and conidia. The number of live yeast cells within macrophages was significantly reduced by activation of macrophages by interferon-gamma (IFN-gamma), while a similar response was not observed with conidia. IFN-gamma-induced macrophage fungicidal activity against yeast cells was mediated by NO and was almost completely inhibited by N(G)-monomethyl-L-arginine (L-NMMA), a competitive inhibitor of NO synthesis, while N(G)-monomethyl-D-arginine (D-NMMA), an optical isomer of L-NMMA, did not show any influence. NO production by macrophages stimulated with IFN-gamma was significantly enhanced when these macrophages were cultured with P. marneffei yeast cells, while conidia did not enhance macrophage NO production. Furthermore, yeast cells were more susceptible to the killing effect of chemically generated NO than conidia. Our results indicate that the yeast form of P. marneffei is more sensitive to the fungicidal activity of IFN-gamma-stimulated macrophages than conidia, and suggest that the different effects of two forms of P. marneffei on macrophage NO production and their different susceptibilities to NO may be reasons for the present findings.

Animals↗
PubMed2001

Functional analysis of the C-terminal cytoplasmic region of the M-factor receptor in fission yeast.

BACKGROUND: Yeast mating-pheromone receptors facilitate the study of G protein-coupled signal transduction. To date, molecular dissection of the budding yeast alpha-factor receptor has been done extensively, but little analysis has been performed with pheromone receptors of fission yeast, another genetically tractable yeast species. RESULTS: We analysed the fission yeast M-factor receptor Map3p. Truncation of the C-terminal 54 amino acids made Map3p dominant-negative over the wild-type. This form, called Map3-dn9p, was competent in the induction of pheromone-dependent gene expression, although it could not direct proper conjugation. Map3-dn9p failed both to provoke the orientated projection of conjugation tubes and to induce adaptation to the pheromone signal associated with endocytosis of the receptor. Deletion and substitution analyses suggested that the integrity of the C-terminal region, rather than a specific subgroup of amino acid residues therein, was vital for the respective Map3p activities. Ubiquitination of the C-terminus was not absolutely essential for Map3p function. CONCLUSIONS: The C-terminal region of Map3p is dispensable for the pheromone signalling per se, but is pivotal for adaptation and pheromone-induced conjugation tube formation, as is true with the budding yeast alpha-factor receptor. However, the mechanisms which induce adaptation appear to differ between fission and budding yeast concerning the necessity of ubiquitination.

Alleles↗
PubMed2000

Virulence of Sporothrix schenckii conidia and yeast cells, and their susceptibility to nitric oxide.

The involvement of nitric oxide (NO) in macrophage (M phi) fungicidal activity against Sporothrix schenckii, and the relationship between NO susceptibility and the differential virulence of conidia and yeast cells, were investigated. Confirming a previously reported correlation between the length of time in culture and virulence of S. schenckii, conidia isolated from 12-day mycelial cultures (Ss-12) were less virulent to mice than conidia from 7-day cultures (Ss-7) or yeast cells. Indicative of NO production, infected animals showed a significant increase in serum levels of nitrite that was lower in mice infected with Ss-12 than in mice infected with Ss-7 or yeast. Stimulation of murine M phi with interferon-gamma (IFN-gamma) induced NO production and inhibition of fungal growth. The cytotoxic activity of M phi against Ss-12 was significantly greater than against Ss-7 or yeast cells, the highly virulent fungal forms. The addition of NO synthase inhibitors abrogated M phi cytotoxic activity against all fungal forms. The phagocytic activity of M phi against Ss-7 was significantly lower than against Ss-12 or yeast cells. Although the ingestion of fungal cells triggered the oxidative burst in M phi, the fungicidal activity was not altered in the presence of superoxide dismutase (SOD) and catalase. In addition, Ss-12 and yeast cells were more susceptible than Ss-7 to the direct fungicidal activity of the NO donors S-nitroso-N-acetyl-DL-penicillamine (SNAP), S-nitrosoglutathione (GSNO) and 3-morpholinosydnonimine (SIN-1). The results of this study indicate that NO is a key cytotoxic mediator involved in the murine M phi defence against S. schenckii, and that the virulence of Ss-7, Ss-12 and yeast cells may be related to a differential susceptibility to NO.

Animals↗
PubMed2001

Effect of lactobacilli on yeast growth, viability and batch and semi-continuous alcoholic fermentation of corn mash.

AIMS: The aim of this study was to evaluate interactions between Saccharomyces cerevisiae and selected strains of lactobacilli regarding cell viabilities, and production of organic acids and ethanol during fermentation. METHODS AND RESULTS: Corn mashes were inoculated with yeasts and selected strains of lactobacilli, and fermented in batch or semi-continuous (cascade) mode. Ethanolic fermentation rates and viabilities of yeast were not affected by lactobacilli unless the mash was pre-cultured with lactobacilli. Then, yeast growth was inhibited and the production of ethanol was reduced by as much as 22%. CONCLUSION: Yeasts inhibited the multiplication of lactobacilli and this resulted in reduced production of acetic and lactic acids. The self-regulating nature of the cascade system allowed the yeast to recover, even when the lactobacilli had a head start, and reduced the size of the population of the contaminating Lactobacillus to a level which had an insignificant effect on fermentation rate or ethanol yield. SIGNIFICANCE AND IMPACT OF THE STUDY: Contamination during fermentation is normally taken care of by the large yeast inoculum, although yeast growth and fermentation rates could be adversely affected by the presence of high numbers of lactobacilli in incoming mash or in transfer lines.

Acetates↗
PubMed1999

Differential expression of an hsp70 gene during transition from the mycelial to the infective yeast form of the human pathogenic fungus Paracoccidioides brasiliensis.

We have isolated and characterized cDNA and genomic clones that encode a 70 kDa heat shock protein (Hsp70) from the dimorphic human pathogenic fungus Paracoccidioides brasiliensis. The gene encodes a 649-amino-acid protein showing high identity with other members of the hsp70 gene family. The hsp70 gene is induced during both heat shock of yeast cells at 42 degrees C and the mycelial to yeast transition. A differential expression of this gene can be observed between mycelial and yeast forms, with a much higher level of expression in the yeast. We found two introns of 178 and 72 nucleotides in the P. brasiliensis hsp70 gene. Splicing of these introns is regulated during the heat shock process and possibly during infection. In order to analyse the differential accumulation of unspliced mRNA following cellular differentiation and/or heat shock, reverse transcriptase-polymerase chain reaction (RT-PCR) experiments were carried out. The temperature-induced mycelial to yeast transition results in the transient accumulation of unspliced hsp70 mRNA transcripts. Yeast cells, after adaptation at 36 degrees C, seem to be more proficient at splicing, at least with respect to hsp70 mRNA because, during a severe heat shock (42 degrees C), the unspliced form of this mRNA does not accumulate. The mycelial to yeast differentiation will have the adaptational effect of increasing the resistance of the organism to environmental stress, which may be necessary for parasite survival in the mammalian host.

Amino Acid Sequence↗
PubMed1999

Functional complementation of yeast vma1 delta cells by a plant subunit A homolog rescues the mutant phenotype and partially restores vacuolar H(+)-ATPase activity.

The ability of a vacuolar H(+)-ATPase (V-ATPase) subunit homolog (subunit A) from plants to rescue the vma mutant phenotype of yeast was investigated as a first step towards investigating the structure and function of plant subunits in molecular detail. Heterologous expression of cotton cDNAs encoding near-identical isoforms of subunit A in mutant vma1 delta yeast cells successfully rescued the mutant vma phenotype, indicating that subunit A of plants and yeast have retained elements essential to V-ATPases during the course of evolution. Although vacuoles become acidified, the plant-yeast hybrid holoenzyme only partially restored V-ATPase activity (approximately 60%) in mutant yeast cells. Domain substitution of divergent N- or C-termini only slightly enhanced V-ATPase activity, whereas swapping both domains acted synergistically, increasing coupled ATP hydrolysis and proton translocation by approximately 22% relative to the native plant subunit. Immunoblot analysis indicated that similar amounts of yeast, plant or plant-yeast chimeric subunits are membrane-bound. These results suggest that subunit A terminal domains contain structural information that impact V-ATPase structure and function.

Adenosine Triphosphate↗