Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2001-5-25
pubmed:abstractText
The major plant plasma membrane H(+)-ATPases fall into two gene categories, subfamilies I and II. However, in many plant tissues, expression of the two subfamilies overlaps, thus precluding individual characterization. Yeast expression of PMA2 and PMA4, representatives of the two plasma membrane H(+)-ATPase subfamilies in Nicotiana plumbaginifolia, has previously shown that (i) the isoforms have distinct enzymatic properties and that (ii) PMA2 is regulated by phosphorylation of its penultimate residue (Thr) and binds regulatory 14-3-3 proteins, resulting in the displacement of the autoinhibitory C-terminal domain. To obtain insights into regulatory differences between the two subfamilies, we have constructed various chimeric proteins in which the 110-residue C-terminal-encoding region of PMA2 was progressively substituted by the corresponding sequence from PMA4. The PMA2 autoinhibitory domain was localized to a region between residues 851 and 915 and could not be substituted by the corresponding region of PMA4. In contrast to PMA2, PMA4 was poorly phosphorylated at its penultimate residue (Thr) and bound 14-3-3 proteins weakly. The only sequence difference around the phosphorylation site is located two residues upstream of the phosphorylated Thr. It is Ser in PMA2 (as in most members of subfamily I) and His in PMA4 (as in most members of subfamily II). Substitution of His by Ser in PMA4 resulted in an enzyme showing increased phosphorylation status, 14-13-3 binding, and ATPase activity, as well as improved yeast growth. The reverse substitution of Ser by His in PMA2 resulted in the failure of this enzyme to complement the absence of yeast H(+)-ATPases. These results show that the two plant H(+)-ATPase subfamilies differ functionally in their regulatory properties.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histidine, http://linkedlifedata.com/resource/pubmed/chemical/PMA1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/PMA2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Threonine, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7017-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11080498-14-3-3 Proteins, pubmed-meshheading:11080498-Adenosine Triphosphatases, pubmed-meshheading:11080498-Amino Acid Sequence, pubmed-meshheading:11080498-Binding Sites, pubmed-meshheading:11080498-Blotting, Western, pubmed-meshheading:11080498-Cell Membrane, pubmed-meshheading:11080498-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11080498-Fungal Proteins, pubmed-meshheading:11080498-Histidine, pubmed-meshheading:11080498-Molecular Sequence Data, pubmed-meshheading:11080498-Multigene Family, pubmed-meshheading:11080498-Mutation, pubmed-meshheading:11080498-Phosphorylation, pubmed-meshheading:11080498-Plant Proteins, pubmed-meshheading:11080498-Plants, pubmed-meshheading:11080498-Plants, Toxic, pubmed-meshheading:11080498-Plasmids, pubmed-meshheading:11080498-Protein Binding, pubmed-meshheading:11080498-Protein Isoforms, pubmed-meshheading:11080498-Protein Structure, Tertiary, pubmed-meshheading:11080498-Proton-Translocating ATPases, pubmed-meshheading:11080498-Recombinant Fusion Proteins, pubmed-meshheading:11080498-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11080498-Sequence Homology, Amino Acid, pubmed-meshheading:11080498-Serine, pubmed-meshheading:11080498-Threonine, pubmed-meshheading:11080498-Tobacco, pubmed-meshheading:11080498-Tyrosine 3-Monooxygenase
pubmed:year
2001
pubmed:articleTitle
The two major plant plasma membrane H+-ATPases display different regulatory properties.
pubmed:affiliation
Unité de Biochimie Physiologique, Université Catholique de Louvain, Croix du Sud 2-20, B-1348 Louvain-la-Neuve, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't