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Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster
The omega (ome) gene product is a modifier of larval cuticle protein 5 and its alleles (and duplicates) in the third instar of Drosophila melanogaster. Using deletion mapping the locus mapped to 70F-71A on the left arm of chromosome 3. A homozygote null mutant (ome (1)) shows a pleiotropic phenotype...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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University of Arizona Library
2005
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1615233/ https://www.ncbi.nlm.nih.gov/pubmed/17119608 |
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author | Chihara, Carol J. Song, Chunyan LaMonte, Greg Fetalvero, Kristina Hinchman, Kristy Phan, Helen Pineda, Mario Robinson, Kelly Schneider, Gregory P. |
author_facet | Chihara, Carol J. Song, Chunyan LaMonte, Greg Fetalvero, Kristina Hinchman, Kristy Phan, Helen Pineda, Mario Robinson, Kelly Schneider, Gregory P. |
author_sort | Chihara, Carol J. |
collection | PubMed |
description | The omega (ome) gene product is a modifier of larval cuticle protein 5 and its alleles (and duplicates) in the third instar of Drosophila melanogaster. Using deletion mapping the locus mapped to 70F-71A on the left arm of chromosome 3. A homozygote null mutant (ome (1)) shows a pleiotropic phenotype that affected the size, developmental time of the flies, and the fertility (or perhaps the behavior) of homozygous mutant males. The omega gene was verified as producing a dipeptidyl peptidase IV (DPPIV) by genetic analysis, substrate specificity and pH optimum. The identity of the gene was confirmed as CG32145 (cytology 70F4) in the Celera Database (Berkeley Drosophila Genome Project), which is consistent with its deletion map position. The genomic structure of the gene is described and the decrease in DPPIV activity in the mutant ome(1) is shown to be due to the gene CG32145 (omega). The D. melanogaster omega DPPIV enzyme was partially purified and characterized. The exons of the ome(1) mutant were sequenced and a base substitution mutation in exon 4 was identified that would yield a truncated protein caused by a stop codon. A preliminary study of the compartmentalization of the omega DPPIV enzyme in several organs is also reported. Abbreviations: / DPPIV: dipeptidyl peptidase IV LCP5 & LCP6: third instar larval cuticle proteins 5 & 6 ome & ome(1): omega locus name (CG32145) and mutant allele in D. melanogaster pNA: paranotroanilide |
format | Text |
id | pubmed-1615233 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | University of Arizona Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-16152332006-11-21 Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster Chihara, Carol J. Song, Chunyan LaMonte, Greg Fetalvero, Kristina Hinchman, Kristy Phan, Helen Pineda, Mario Robinson, Kelly Schneider, Gregory P. J Insect Sci Articles The omega (ome) gene product is a modifier of larval cuticle protein 5 and its alleles (and duplicates) in the third instar of Drosophila melanogaster. Using deletion mapping the locus mapped to 70F-71A on the left arm of chromosome 3. A homozygote null mutant (ome (1)) shows a pleiotropic phenotype that affected the size, developmental time of the flies, and the fertility (or perhaps the behavior) of homozygous mutant males. The omega gene was verified as producing a dipeptidyl peptidase IV (DPPIV) by genetic analysis, substrate specificity and pH optimum. The identity of the gene was confirmed as CG32145 (cytology 70F4) in the Celera Database (Berkeley Drosophila Genome Project), which is consistent with its deletion map position. The genomic structure of the gene is described and the decrease in DPPIV activity in the mutant ome(1) is shown to be due to the gene CG32145 (omega). The D. melanogaster omega DPPIV enzyme was partially purified and characterized. The exons of the ome(1) mutant were sequenced and a base substitution mutation in exon 4 was identified that would yield a truncated protein caused by a stop codon. A preliminary study of the compartmentalization of the omega DPPIV enzyme in several organs is also reported. Abbreviations: / DPPIV: dipeptidyl peptidase IV LCP5 & LCP6: third instar larval cuticle proteins 5 & 6 ome & ome(1): omega locus name (CG32145) and mutant allele in D. melanogaster pNA: paranotroanilide University of Arizona Library 2005-11-02 /pmc/articles/PMC1615233/ /pubmed/17119608 Text en Copyright © 2005. Open access; copyright is maintained by the authors. |
spellingShingle | Articles Chihara, Carol J. Song, Chunyan LaMonte, Greg Fetalvero, Kristina Hinchman, Kristy Phan, Helen Pineda, Mario Robinson, Kelly Schneider, Gregory P. Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster |
title | Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster |
title_full | Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster |
title_fullStr | Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster |
title_full_unstemmed | Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster |
title_short | Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster |
title_sort | identification and partial characterization of the enzyme of omega: one of five putative dpp iv genes in drosophila melanogaster |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1615233/ https://www.ncbi.nlm.nih.gov/pubmed/17119608 |
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