Linked Life Data

9154989

Source:http://linkedlifedata.com/resource/pubmed/id/9154989

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-6-23
pubmed:databankReference
pubmed:abstractText
The mammalian Nramp1 protein is an integral membrane protein expressed exclusively in macrophages, where it plays a critical role in the ability of these cells to destroy ingested microbes. The bactericidal mechanism of action of Nramp1 remains unknown. We report the identification and characterization of cDNA clones corresponding to three homologues of the mammalian Nramp1 gene from the genome of Oryza sativa, OsNramp1, OsNramp2, and OsNramp3. These three genes encode a novel group of highly similar hydrophobic polypeptides sharing between 64% and 75% sequence similarity, that show similar hydropathy profiles, and predicted secondary structure, including the same number, position, and sequence characteristics (including conserved charges) of transmembrane domains. Together, these define a highly conserved membrane associated hydrophobic core. The three plant proteins show a remarkable degree of sequence similarity with their mammalian counterpart (60% to 70% similarity), including primary and secondary structure elements previously described in ion transporters and channels. Expression studies in normal plant tissues indicate that while OsNramp1 is expressed primarily in roots, and OsNramp2 is primarily expressed in leaves, OsNramp3 is expressed in both tissues. The recent discovery that the yeast Nramp homologue SMF1 functions as a manganese transporter raises the exciting possibility that OsNramp encodes a family of metal ion transporters in plants.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1085-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9154989-Amino Acid Sequence, pubmed-meshheading:9154989-Base Sequence, pubmed-meshheading:9154989-Biological Transport, pubmed-meshheading:9154989-Carrier Proteins, pubmed-meshheading:9154989-Cation Transport Proteins, pubmed-meshheading:9154989-Cloning, Molecular, pubmed-meshheading:9154989-Conserved Sequence, pubmed-meshheading:9154989-Gene Expression Regulation, Plant, pubmed-meshheading:9154989-Genes, Plant, pubmed-meshheading:9154989-Ions, pubmed-meshheading:9154989-Membrane Proteins, pubmed-meshheading:9154989-Membrane Transport Proteins, pubmed-meshheading:9154989-Metals, pubmed-meshheading:9154989-Molecular Sequence Data, pubmed-meshheading:9154989-Oryza sativa, pubmed-meshheading:9154989-Plant Proteins, pubmed-meshheading:9154989-RNA, Messenger, pubmed-meshheading:9154989-RNA, Plant, pubmed-meshheading:9154989-Sequence Analysis, DNA, pubmed-meshheading:9154989-Sequence Homology, Amino Acid
pubmed:year
1997
pubmed:articleTitle
Cloning and characterization of the OsNramp family from Oryza sativa, a new family of membrane proteins possibly implicated in the transport of metal ions.
pubmed:affiliation
Department of Biochemistry, McGill University, Montréal Québec, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't