Linked Life Data

16903865

Source:http://linkedlifedata.com/resource/pubmed/id/16903865

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2006-8-30
pubmed:abstractText
Alr1p is an integral plasma membrane protein essential for uptake of Mg(2+) into yeast cells. Homologs of Alr1p are restricted to fungi and some protozoa. Alr1-type proteins are distant relatives of the mitochondrial and bacterial Mg(2+)-transport proteins, Mrs2p and CorA, respectively, with which they have two adjacent TM domains and a short Mg(2+) signature motif in common. The yeast genome encodes a close homolog of Alr1p, named Alr2p. Both proteins are shown here to be present in the plasma membrane. Alr2p contributes poorly to Mg(2+) uptake. Substitution of a single arginine with a glutamic acid residue in the loop connecting the two TM domains at the cell surface greatly improves its function. Both proteins are shown to form homo-oligomers as well as hetero-oligomers. Wild-type Alr2p and mutant Alr1 proteins can have dominant-negative effects on wild-type Alr1p activity, presumably through oligomerization of low-function with full-function proteins. Chemical cross-linking indicates the presence of Alr1 oligomers, and split-ubiquitin assays reveal Alr1p-Alr1p, Alr2p-Alr2p, and Alr1p-Alr2p interactions. These assays also show that both the N-terminus and C-terminus of Alr1p and Alr2p are exposed to the inner side of the plasma membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1742-464X
pubmed:author
pubmed:issnType
Print
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4236-49
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Oligomerization of the Mg2+-transport proteins Alr1p and Alr2p in yeast plasma membrane.
pubmed:affiliation
Max F. Perutz Laboratories, Department of Genetics, University of Vienna, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't