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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
41
|
| pubmed:dateCreated |
1994-11-17
|
| pubmed:databankReference | |
| pubmed:abstractText |
Porins are voltage-gated diffusion pores found in all eukaryotic kingdoms. Here we describe, for the first time, the identification and characterization of two cDNAs encoding porins from plants. Peptide sequences obtained from a 30-kDa protein of envelope membranes from pea root plastids allowed the isolation of two cDNA clones from pea and maize. On the protein level, both proteins are homologous by 58%. Sequence comparison against the Swiss-Prot sequence data base revealed a homology of about 25% to mitochondrial porins from fungi and human. Computer-aided predictions of the secondary structure of the plant porins revealed the presence of 16 antiparallel beta-strands that are also found in mitochondrial porins. Porins from non-green plastids and from the outer mitochondrial membrane were reconstituted into planar lipid bilayers. The proteins showed high pore-forming activities and similar single-channel conductances. In vitro translated porin was preferentially imported only into non-green plastids but not into chloroplasts. To our knowledge, this is the first example of selective import of a plastid protein into different types of plastids. This finding is in line with the observation that an immunoreactive 30-kDa band was only found in non-green plastids and mitochondria but not in chloroplasts. We conclude that mitochondria and non-green plastids possess homologous porin proteins, whereas chloroplasts are characterized by a different type of porin.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Porins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
14
|
| pubmed:volume |
269
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
N
|
| pubmed:pagination |
25754-60
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7523392-Amino Acid Sequence,
pubmed-meshheading:7523392-Biological Markers,
pubmed-meshheading:7523392-Biological Transport,
pubmed-meshheading:7523392-Cell Compartmentation,
pubmed-meshheading:7523392-Cell Fractionation,
pubmed-meshheading:7523392-Cloning, Molecular,
pubmed-meshheading:7523392-DNA, Complementary,
pubmed-meshheading:7523392-Genes, Plant,
pubmed-meshheading:7523392-Intracellular Membranes,
pubmed-meshheading:7523392-Ion Channels,
pubmed-meshheading:7523392-Lipid Bilayers,
pubmed-meshheading:7523392-Mitochondria,
pubmed-meshheading:7523392-Molecular Sequence Data,
pubmed-meshheading:7523392-Multigene Family,
pubmed-meshheading:7523392-Peas,
pubmed-meshheading:7523392-Plant Proteins,
pubmed-meshheading:7523392-Plant Roots,
pubmed-meshheading:7523392-Plastids,
pubmed-meshheading:7523392-Porins,
pubmed-meshheading:7523392-Protein Biosynthesis,
pubmed-meshheading:7523392-Protein Structure, Secondary,
pubmed-meshheading:7523392-Sequence Analysis,
pubmed-meshheading:7523392-Sequence Homology, Amino Acid,
pubmed-meshheading:7523392-Vegetables,
pubmed-meshheading:7523392-Zea mays
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Porins from plants. Molecular cloning and functional characterization of two new members of the porin family.
|
| pubmed:affiliation |
Julius-von-Sachs-Institut für Biowissenschaften, Universität Würzburg, Federal Republic of Germany.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|