Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Chihara, Carol J., Song, Chunyan, LaMonte, Greg, Fetalvero, Kristina, Hinchman, Kristy, Phan, Helen, Pineda, Mario, Robinson, Kelly, Schneider, Gregory P.
Formato: Texto
Lenguaje:English
Publicado: University of Arizona Library 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1615233/
https://www.ncbi.nlm.nih.gov/pubmed/17119608
_version_ 1782130482975080448
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
work_keys_str_mv AT chiharacarolj identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT songchunyan identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT lamontegreg identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT fetalverokristina identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT hinchmankristy identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT phanhelen identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT pinedamario identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT robinsonkelly identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster
AT schneidergregoryp identificationandpartialcharacterizationoftheenzymeofomegaoneoffiveputativedppivgenesindrosophilamelanogaster