Linked Life Data

10353834

Source:http://linkedlifedata.com/resource/pubmed/id/10353834

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1999-6-23
pubmed:abstractText
The plasma membrane H+-ATPase is a proton pump belonging to the P-type ATPase superfamily and is important for nutrient acquisition in plants. The H+-ATPase is controlled by an autoinhibitory C-terminal regulatory domain and is activated by 14-3-3 proteins which bind to this part of the enzyme. Alanine-scanning mutagenesis through 87 consecutive amino acid residues was used to evaluate the role of the C-terminus in autoinhibition of the plasma membrane H+-ATPase AHA2 from Arabidopsis thaliana. Mutant enzymes were expressed in a strain of Saccharomyces cerevisiae with a defective endogenous H+-ATPase. The enzymes were characterized by their ability to promote growth in acidic conditions and to promote H+ extrusion from intact cells, both of which are measures of plasma membrane H+-ATPase activity, and were also characterized with respect to kinetic properties such as affinity for H+ and ATP. Residues that when altered lead to increased pump activity group together in two regions of the C-terminus. One region stretches from K863 to L885 and includes two residues (Q879 and R880) that are conserved between plant and fungal H+-ATPases. The other region, incorporating S904 to L919, is situated in an extension of the C-terminus unique to plant H+-ATPases. Alteration of residues in both regions led to increased binding of yeast 14-3-3 protein to the plasma membrane of transformed cells. Taken together, our data suggest that modification of residues in two regions of the C-terminal regulatory domain exposes a latent binding site for activatory 14-3-3 proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7227-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10353834-14-3-3 Proteins, pubmed-meshheading:10353834-Amino Acid Sequence, pubmed-meshheading:10353834-Amino Acid Substitution, pubmed-meshheading:10353834-Arabidopsis, pubmed-meshheading:10353834-Cell Membrane, pubmed-meshheading:10353834-Enzyme Activation, pubmed-meshheading:10353834-Enzyme Inhibitors, pubmed-meshheading:10353834-Isoenzymes, pubmed-meshheading:10353834-Kinetics, pubmed-meshheading:10353834-Molecular Sequence Data, pubmed-meshheading:10353834-Mutagenesis, Insertional, pubmed-meshheading:10353834-Mutagenesis, Site-Directed, pubmed-meshheading:10353834-Peptide Fragments, pubmed-meshheading:10353834-Peptide Mapping, pubmed-meshheading:10353834-Proteins, pubmed-meshheading:10353834-Proton-Translocating ATPases, pubmed-meshheading:10353834-Saccharomyces cerevisiae, pubmed-meshheading:10353834-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10353834-Tyrosine 3-Monooxygenase
pubmed:year
1999
pubmed:articleTitle
Molecular dissection of the C-terminal regulatory domain of the plant plasma membrane H+-ATPase AHA2: mapping of residues that when altered give rise to an activated enzyme.
pubmed:affiliation
Department of Plant Biology, The Royal Veterinary and Agricultural University, Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't