Source:http://linkedlifedata.com/resource/pubmed/id/14604798
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
2003-11-7
|
| pubmed:databankReference | |
| pubmed:abstractText |
The protein called voltage-dependent anion-selective channel (VDAC), or mitochondrial porin, forms channels that provide the major pathway for small metabolites across the mitochondrial outer membrane. We have identified and sequenced agporin, a gene of the malaria vector mosquito Anopheles gambiae that conceptually encodes a protein with 73% identity to the VDAC protein encoded by the porin gene in Drosophila melanogaster. By in situ hybridization, we have localized agporin at region 35D on the right arm of A. gambiae chromosome 3, which is homologous to the 2L chromosomal arm of D. melanogaster where the porin gene resides. The comparison of agporin with its putative Drosophila counterpart revealed that both the nucleotide sequence and the structural organization of the two genes are strikingly conserved even though the ancestral lines of A. gambiae and D. melanogaster are thought to have diverged about 250 million years ago. Our results suggest that, while in yeast, plants, and mammals, VDAC isoforms are encoded by small multigene families and are able to compensate for each other at least partially, in A. gambiae a single gene encodes the VDAC protein.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/Voltage-Dependent Anion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/porin protein, Drosophila
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0378-1119
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
23
|
| pubmed:volume |
317
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
111-5
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:14604798-Amino Acid Sequence,
pubmed-meshheading:14604798-Animals,
pubmed-meshheading:14604798-Anopheles,
pubmed-meshheading:14604798-DNA,
pubmed-meshheading:14604798-DNA, Complementary,
pubmed-meshheading:14604798-Drosophila Proteins,
pubmed-meshheading:14604798-Drosophila melanogaster,
pubmed-meshheading:14604798-Exons,
pubmed-meshheading:14604798-Genes, Insect,
pubmed-meshheading:14604798-In Situ Hybridization,
pubmed-meshheading:14604798-Insect Proteins,
pubmed-meshheading:14604798-Introns,
pubmed-meshheading:14604798-Molecular Sequence Data,
pubmed-meshheading:14604798-Porins,
pubmed-meshheading:14604798-Sequence Alignment,
pubmed-meshheading:14604798-Sequence Analysis, DNA,
pubmed-meshheading:14604798-Sequence Homology, Amino Acid,
pubmed-meshheading:14604798-Voltage-Dependent Anion Channels
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
A comparative study of the porin genes encoding VDAC, a voltage-dependent anion channel protein, in Anopheles gambiae and Drosophila melanogaster.
|
| pubmed:affiliation |
Dipartimento di Anatomia Patologica e di Genetica, sezione di Genetica, Università di Bari, via Amendola 165/A, Bari 70126, Italy.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|