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VMA1 Vma1p

VMA1, VMA1-derived endonuclease, TFP1
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ATPase, V-ATPase, CAN, ACID, HAD
Papers using VMA1 antibodies
Structural Insights of the Nucleotide-Dependent Conformational Changes of Thermotoga maritima MutL Using Small-Angle X-ray Scattering Analysis.
Marinus Martin G., In PLoS ONE, 2008
... MutL was cloned as a direct fusion with the Sce VMA1 Intein-tag in the pTYB1 plasmid [24] (New England Biolabs, Inc) ...
Papers on VMA1
Tfp1 is required for ion homeostasis, fluconazole resistance and N-Acetylglucosamine utilization in Candida albicans.
Li et al., Tianjin, China. In Biochim Biophys Acta, Oct 2015
In this study, we demonstrated the essential roles of V-ATPase through Tfp1, a putative V-ATPase subunit.
Coordinated gene regulation in the initial phase of salt stress adaptation.
Proft et al., Valencia, Spain. In J Biol Chem, May 2015
Loss of function of the vacuolar H(+)-ATPase (vma1) or a defect in the biosynthesis of the osmolyte glycerol (gpd1) caused a prolonged repression of housekeeping genes and a delay in gene activation at inducible loci.
Role of TFP1 in vacuolar acidification, oxidative stress and filamentous development in Candida albicans.
Li et al., Tianjin, China. In Fungal Genet Biol, 2014
In this study, we identified C. albicans Tfp1 as a putative subunit of V-ATPase, and explored its importance in multiple cellular processes.
Cloning Rosa hybrid phenylacetaldehyde synthase for the production of 2-phenylethanol in a whole cell Escherichia coli system.
Fishman et al., Haifa, Israel. In Appl Microbiol Biotechnol, 2014
The desired results were obtained by using the pTYB21 plasmid containing the intein tag from the Saccharomyces cerevisiae VMA1.
Selection and evaluation of reference genes for expression studies with quantitative PCR in the model fungus Neurospora crassa under different environmental conditions in continuous culture.
Biffinger et al., Washington, D.C., United States. In Plos One, 2013
Based on combined stability values from NormFinder and Best Keeper software packages, the following are the most appropriate reference genes under conditions of: (1) light/dark cycling: btl, asl, and vma1; (2) all-dark growth: btl, tbp, vma1, and vma2; (3) temperature flux: btl, vma1, act, and asl; (4) all conditions combined: vma1, vma2, tbp, and btl.
A new fusion protein platform for quantitatively measuring activity of multiple proteases.
Fan et al., Hefei, China. In Microb Cell Fact, 2013
RESULTS: We tested seven different protease cleavage sequences (rhinovirus 3C, TEV protease, factor Xa, Ssp DnaB intein, Sce VMA1 intein, thrombin and enterokinase), three different tags (His6, GST, CBD and MBP) and two different DALs (eDAL and sDAL), for their performance as substrate to the seven corresponding proteases.
Acidosis-induced V-ATPase trafficking in salivary ducts is initiated by cAMP/PKA/CREB pathway via regulation of Rab11b expression.
Roussa et al., Freiburg, Germany. In Int J Biochem Cell Biol, 2012
Data show that the cAMP/PKA/CREB signaling pathway initiates acidosis-induced V-ATPase trafficking in salivary ducts via regulation of Rab11b expression.
Sequence and analysis of the genome of the pathogenic yeast Candida orthopsilosis.
Butler et al., Dublin, Ireland. In Plos One, 2011
We also show that an intein in the vacuolar ATPase gene VMA1 is present in C. orthopsilosis but not C. parapsilosis, and has a patchy distribution in Candida species.
A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast.
Serrano et al., Sevilla, Spain. In Biochem J, 2011
Phenotypic complementation was achieved both with a yeast strain with its V-ATPase specifically inhibited by bafilomycin A1 and with a vma1-null mutant lacking a catalytic V-ATPase subunit.
Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts.
Roussa et al., Freiburg, Germany. In J Cell Physiol, 2011
These data introduce Rab11b as a crucial regulator and Rip11 as mediator of acidosis-induced V-ATPase traffic in duct cells of submandibular gland.
Proteomic analysis of dorsolateral prefrontal cortex indicates the involvement of cytoskeleton, oligodendrocyte, energy metabolism and new potential markers in schizophrenia.
Dias-Neto et al., São José dos Campos, Brazil. In J Psychiatr Res, 2009
This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
Proteome analysis of schizophrenia patients Wernicke's area reveals an energy metabolism dysregulation.
Dias-Neto et al., São Paulo, Brazil. In Bmc Psychiatry, 2008
This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia.
Reflections on protein splicing: structures, functions and mechanisms.
Satow et al., Tokyo, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2008
VMA1 consists of a single open reading frame and contains two independent genetic information for Vma1p (a catalytic 70-kDa subunit of the vacuolar H(+)-ATPase) and VDE (a 50-kDa DNA endonuclease) as an in-frame spliced insert in the gene.
Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump.
Gluck et al., San Francisco, United States. In J Biol Chem, 2007
there is an important role for physical association between aldolase and the A, B and E subunits of V-ATPase in the regulation of the proton pump
Protein splicing: its discovery and structural insight into novel chemical mechanisms.
Satow et al., Uenohara, Japan. In Iubmb Life, 2005
VMA1 consists of a single open reading frame and yet comprises two independent genetic information for Vma1p (a catalytic 70-kDa subunit of the vacuolar H+-ATPase) and VDE (a 50-kDa DNA endonuclease) as an in-frame spliced insert in the gene.
Molecular mechanism of VDE-initiated intein homing in yeast nuclear genome.
Ohya et al., Kashiwa, Japan. In Adv Biophys, 2003
In Saccharomyces cerevisiae, VMA1 intein encodes a homing endonuclease termed VDE which is produced by an autocatalytic protein splicing reaction.
Protein splicing: its chemistry and biology.
Anraku, Tokyo, Japan. In Genes Cells, 1997
This unique autocatalytic reaction was first discovered in the yeast VMA1 protein, a 120kDa spliced polypeptide encoded by the VMA1 gene of Saccharomyces cerevisiae.
Protozyme: emerging evidence in nature.
Hirata et al., Tokyo, Japan. In J Biochem, 1994
The VMA1 locus in Saccharomyces cerevisiae contains a nested genetic element, the VDE gene, and expresses two functional proteins.
Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae.
Thorner et al., Berkeley, United States. In Nature, 1992
The site cleaved by the VMA1-derived endonuclease exists in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame.
Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase.
Stevens et al., Eugene, United States. In Science, 1990
The TFP1 gene of the yeast Saccharomyces cerevisiae encodes two proteins: the 69-kilodalton (kD) catalytic subunit of the vacuolar proton-translocating adenosine triphosphatase (H(+)-ATPase) and a 50-kD protein.
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