Linked Life Data

12182706

Source:http://linkedlifedata.com/resource/pubmed/id/12182706

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-8-16
pubmed:databankReference
pubmed:abstractText
Using the two-hybrid technique we identified a novel protein whose N-terminal 88 amino acids (aa) interact with the C-terminal regulatory domain of the plasma membrane (PM) H+-ATPase from Arabidopsis thaliana (aa 847-949 of isoform AHA1). The corresponding gene has been named Ppi1 for Proton pump interactor 1. The encoded protein is 612 aa long and rich in charged and polar residues, except for the extreme C-terminus, where it presents a hydrophobic stretch of 24 aa. Several genes in the A. thaliana genome and many ESTs from different plant species share significant similarity (50-70% at the aa level over stretches of 200-600 aa) to Ppi1. The PPI1 N-terminus, expressed in bacteria as a fusion protein with either GST or a His-tag, binds the PM H+-ATPase in overlay experiments. The same fusion proteins and the entire coding region fused to GST stimulate H+-ATPase activity. The effect of the His-tagged peptide is synergistic with that of fusicoccin (FC) and of tryptic removal of a C-terminal 10 kDa fragment. The His-tagged peptide binds also the trypsinised H+-ATPase. Altogether these results indicate that PPI1 N-terminus is able to modulate the PM H+-ATPase activity by binding to a site different from the 14-3-3 binding site and is located upstream of the trypsin cleavage site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0960-7412
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
487-97
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12182706-14-3-3 Proteins, pubmed-meshheading:12182706-Amino Acid Sequence, pubmed-meshheading:12182706-Arabidopsis, pubmed-meshheading:12182706-Arabidopsis Proteins, pubmed-meshheading:12182706-Base Sequence, pubmed-meshheading:12182706-Carrier Proteins, pubmed-meshheading:12182706-Cell Membrane, pubmed-meshheading:12182706-Enzyme Activation, pubmed-meshheading:12182706-Glycosides, pubmed-meshheading:12182706-Isoenzymes, pubmed-meshheading:12182706-Molecular Sequence Data, pubmed-meshheading:12182706-Proton Pumps, pubmed-meshheading:12182706-Proton-Translocating ATPases, pubmed-meshheading:12182706-Recombinant Fusion Proteins, pubmed-meshheading:12182706-Sequence Homology, Amino Acid, pubmed-meshheading:12182706-Trypsin, pubmed-meshheading:12182706-Two-Hybrid System Techniques, pubmed-meshheading:12182706-Tyrosine 3-Monooxygenase
pubmed:year
2002
pubmed:articleTitle
A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on H+-ATPase activity differ from those of 14-3-3 proteins.
pubmed:affiliation
Dipartimento di Biologia L. Gorini, Sezione di Fisiologia e Biochimica delle Piante, Centro di Studio CNR-Biologia Cellulare e Molecolare delle Piante, c/o Dip. di Biologia, Via Celoria 26, 20133 Milan, Italy. piero.morandini@unimi.it
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't