Source:http://linkedlifedata.com/resource/pubmed/id/10354468
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1999-8-2
|
| pubmed:databankReference | |
| pubmed:abstractText |
We have isolated mutations in the gene Drosophila methionine aminopeptidase 2 (DMAP2), which encodes a homolog of the type 2 methionine aminopeptidase from yeast, also known as the eukaryotic initiation factor 2alpha (eIF2alpha) associated protein p67. Weak DMAP2 mutations cause ommatidial rotation defects and loss of ventral tissue in the compound eye as well as extra wing veins, whereas stronger alleles impair tissue growth. These limited phenotypes, in conjunction with the differential accumulation of DMAP2 transcripts throughout embryonic and larval development, suggest that a subset of proteins is spatially and temporally regulated at the level of post-translational processing or translation initiation during development. These results provide genetic evidence for post-transcriptional control in the development of multicellular organisms.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0925-4773
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
82
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
23-8
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10354468-Amino Acid Sequence,
pubmed-meshheading:10354468-Aminopeptidases,
pubmed-meshheading:10354468-Animals,
pubmed-meshheading:10354468-Body Patterning,
pubmed-meshheading:10354468-Cell Division,
pubmed-meshheading:10354468-Drosophila Proteins,
pubmed-meshheading:10354468-Drosophila melanogaster,
pubmed-meshheading:10354468-Eye,
pubmed-meshheading:10354468-Female,
pubmed-meshheading:10354468-Genes, Insect,
pubmed-meshheading:10354468-Glycoproteins,
pubmed-meshheading:10354468-Male,
pubmed-meshheading:10354468-Molecular Sequence Data,
pubmed-meshheading:10354468-Mutation,
pubmed-meshheading:10354468-Peptide Chain Initiation, Translational,
pubmed-meshheading:10354468-Phenotype,
pubmed-meshheading:10354468-Sequence Homology, Amino Acid,
pubmed-meshheading:10354468-Wing
|
| pubmed:year |
1999
|
| pubmed:articleTitle |
A methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in Drosophila.
|
| pubmed:affiliation |
Laboratory of Developmental Neurogenetics, The Rockefeller University, 1230 York Avenue, Box 248, New York, NY 10021, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|