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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

PMA1 Pma1p

PMA1, Pma1p
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Top mentioned proteins: ATPase, ACID, CAN, HAD, V1a
Papers on PMA1
Selection and validation of reference genes for quantitative real-time PCR studies during Saccharomyces cerevisiae alcoholic fermentation in the presence of sulfite.
Corich et al., Padova, Italy. In Int J Food Microbiol, Jan 2016
Among 15 reference genes tested ALG9, FBA1, UBC6 and PFK1 appeared to be the most reliable while ENO1, PMA1, DED1 and FAS2 were the worst.
Cu/Zn superoxide dismutase and the proton ATPase Pma1p of Saccharomyces cerevisiae.
Culotta et al., Baltimore, United States. In Biochem Biophys Res Commun, Aug 2015
We recently demonstrated a function for Saccharomyces cerevisiae Sod1p in signaling through CK1γ casein kinases and identified the essential proton ATPase Pma1p as one likely target.
Pma1 is an alkali/alkaline earth metal cation ATPase that preferentially transports Na(+) and K(+) across the Mycobacterium smegmatis plasma membrane.
Soto et al., Bogotá, Colombia. In Microbiol Res, Jul 2015
Mycobacterium smegmatis Pma1 is the orthologue of M. tuberculosis P-type ATPase cation transporter CtpF, which is activated under stress conditions, such as hypoxia, starvation and response to antituberculous and toxic substances.
Specific Activation of the Plant P-type Plasma Membrane H+-ATPase by Lysophospholipids Depends on the Autoinhibitory N- and C-terminal Domains.
Palmgren et al., Frederiksberg, Denmark. In J Biol Chem, Jul 2015
Here we show that lysophospholipids specifically activate a plant plasma membrane H(+)-ATPase (Arabidopsis thaliana AHA2) by a mechanism that involves both cytoplasmic terminal domains of AHA2, whereas they have no effect on the fungal counterpart (Saccharomyces cerevisiae Pma1p).
Nutrient transport into germinating Trichoderma atroviride conidia and development of its driving force.
Varečka et al., Bratislava, Slovakia. In Microbiology, Jun 2015
(14)C-valine uptake was also measured into a mutant with disrupted pma1 gene.
Too much of a good thing: the unique and repeated paths toward copper adaptation.
Otto et al., Vancouver, Canada. In Genetics, Feb 2015
Four other genes received multiple, independent mutations in different lines (the vacuolar transporter genes VTC1 and VTC4; the plasma membrane H+-ATPase PMA1; and MAM3, a protein required for normal mitochondrial morphology).
Sir2 phosphorylation through cAMP-PKA and CK2 signaling inhibits the lifespan extension activity of Sir2 in yeast.
Kim et al., Taejŏn, South Korea. In Elife, 2014
Sir2 partially represses the transcription of lifespan-associated genes, such as PMA1 (encoding an H(+)-ATPase) and many ribosomal protein genes, through deacetylation of Lys 16 of histone H4 in the promoter regions of these genes.
Mechanism of proanthocyanidins-induced alcoholic fermentation enhancement in Saccharomyces cerevisiae.
Huang et al., Qingdao, China. In J Ind Microbiol Biotechnol, 2014
At Day 0.5 the gene expression level of PMA1 in AWRI R2 strain supplemented with 1.0 mg/mL PAs was decreased by around 54 % with a 50 % and a 56.5 % increase in the concentration of intracellular ATP and NADH/NAD(+) ratio, respectively, compared to that of control.
Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p.
Kane et al., Syracuse, United States. In J Biol Chem, 2014
Yeast mutants lacking the intracellular V-ATPase proton pump (vma mutants) have reduced levels of the Pma1p proton pump at the plasma membrane and increased levels in organelles including the vacuolar lumen.
The DosR dormancy regulator of Mycobacterium tuberculosis stimulates the Na(+)/K (+) and Ca (2+) ATPase activities in plasma membrane vesicles of mycobacteria.
Soto et al., Bogotá, Colombia. In Curr Microbiol, 2014
We performed bioinformatic analyses which indicated that the pma1 gene product is the M. smegmatis ortholog of the M. tuberculosis cation transporter CtpF.
The underlying structure of adaptation under strong selection in 12 experimental yeast populations.
Anderson et al., Toronto, Canada. In Eukaryot Cell, 2014
In a high-salt environment, a broad target of 11 mutations within the proton exporter, PMA1, was observed among the six populations, in addition to expansions of the ENA gene cluster.
A new pma1 mutation identified in a chronologically long-lived fission yeast mutant.
Aiba et al., Nagoya, Japan. In Febs Open Bio, 2013
We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1 (+) that encoded for an essential P-type proton ATPase.
Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast.
Malhotra et al., Barcelona, Spain. In Mol Biol Cell, 2012
Findings highlight the conserved role of cofilin and SPCA1/Pmr1 in sorting of the soluble secretory proteins at the trans-Golgi network/late Golgi membranes in eukaryotes.
Yeast Swd2 is essential because of antagonism between Set1 histone methyltransferase complex and APT (associated with Pta1) termination factor.
Buratowski et al., Boston, United States. In J Biol Chem, 2012
Data suggest that ecruitment of COMPASS subunits PMA1 and RPS13 is dependent upon Set1 and Swd2, a subunit of the essential transcription termination factor APT (associated with Pta1).
Cellular effects and epistasis among three determinants of adaptation in experimental populations of Saccharomyces cerevisiae.
Anderson et al., Toronto, Canada. In Eukaryot Cell, 2011
Negative interaction between PMA1e and MKT1e is mediated by alterations in intracellular pH.
Gene expression profiling of yeasts overexpressing wild type or misfolded Pma1 variants reveals activation of the Hog1 MAPK pathway.
Portillo et al., Madrid, Spain. In Mol Microbiol, 2011
Hog1-mitogen-activated protein kinase pathway is activated by both wild type and mutantPma1.
Point mutations in Pma1 H+-ATPase of Saccharomyces cerevisiae: influence on its expression and activity.
Petrov, Moscow, Russia. In Biochemistry (mosc), 2010
Point mutations in Pma1 H+-ATPase of Saccharomyces cerevisiae: influence on its expression and activity
Biogenesis and function of the yeast plasma-membrane H(+)-ATPase.
Slayman et al., New Haven, United States. In J Exp Biol, 2000
This paper reviews three phenotypically distinct classes of mutant that have resulted from work on the yeast PMA1 H(+)-ATPase: (1) mutant ATPases that are poorly folded and retained in the endoplasmic reticulum; (2) mutants in which the conformational equilibrium has been shifted from the E(2) state, characterized by high affinity for vanadate, to the E(1) state, characterized by high affinity for ATP; and (3) mutants with altered coupling between ATP hydrolysis and proton pumping.
The plasma membrane H(+)-ATPase of fungi. A candidate drug target?
Monk et al., New York City, United States. In Ann N Y Acad Sci, 1997
Secondly, the well-characterized biochemistry and genetics of the H(+)-ATPase (encoded by the PMA1 gene) facilitate detailed analysis of interaction of lead or model compounds with the enzyme.
Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases.
Fink et al., In Nature, 1986
We have cloned, mapped and sequenced the gene encoding the yeast plasma membrane ATPase (PMA1) and report here that it maps to chromosome VII adjacent to LEU1.
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