Polytene chromosome maps in the Medfly <i>Ceratitis capitata</i>

Zacharopoulou, A.

doi:10.1139/g90-030

Cited by 85 publications

(127 citation statements)

References 19 publications

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“…The Benakeion mass rearing strain of C. capitata, having the standard gene arrangement (Zacharopoulou, 1990), was used in this study. This strain has been maintained in our laboratory for more than 25 years under standard conditions (25 ± 1°C, 40-50% relative humidity and 12 h light:12 h dark photoperiod) as previously described (Mintzas et al, 1983).…”

Section: Animals and Developmental Stagingmentioning

confidence: 99%

“…High levels of zygotic CcPSMA5 Salivary gland polytene chromosomes from 120-h-old larvae were analyzed by fluorescence in situ hybridization using as a probe the CcPSMA5 cDNA as described in Materials and Methods. The hybridization signal is indicated by an arrow at the 44B region of the 4th chromosome (Zacharopoulou, 1990).…”

Section: Developmental Expression Of Ccpsma5 Mrna In Whole Animalsmentioning

confidence: 99%

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cDNA cloning, characterization, and developmental expression of the 20S proteasome α5 subunit in the Mediterranean fruit fly Ceratitis capitata

Verras

Gourzi

Kalosaka

et al. 2007

Arch Insect Biochem Physiol

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In the present study, we report the cDNA cloning, characterization, and developmental expression of the 20S proteasome alpha5 subunit from the Mediterranean fruit fly Ceratitis capitata (medfly). Using an RT-PCR fragment that corresponds to the amino-terminal region of the Drosophila melanogaster 20S proteasome alpha5 subunit, we isolated a 987-bp cDNA that encodes the complete coding region of the medfly ortholog, which was named CcPSMA5. CcPSMA5 consists of 241 amino acids and has a predicted molecular weight of 26.4 kDa and pI 4.75. Comparison of the CcPSMA5 amino acid sequence with the sequences of all known 20S proteasome alpha5 subunits from different organisms indicated that the medfly 20S proteasome alpha5 subunit has the strongest homology to that of Drosophila. In situ hybridization showed that the CcPSMA5 gene is mapped in the region 44B of chromosome 4. Northern blot hybridization analysis showed that the CcPSMA5 mRNA has a size of approximately 1.2 kb. High levels of the CcPSMA5 mRNA were detected in freshly laid eggs, indicating that they were maternally deposited. The mRNA expression pattern during medfly development suggests that the CcPSMA5 gene is upregulated before mid-embryogenesis and at the onset of metamorphosis.

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Section: Animals and Developmental Stagingmentioning

confidence: 99%

Section: Developmental Expression Of Ccpsma5 Mrna In Whole Animalsmentioning

confidence: 99%

cDNA cloning, characterization, and developmental expression of the 20S proteasome α5 subunit in the Mediterranean fruit fly Ceratitis capitata

Verras

Gourzi

Kalosaka

et al. 2007

Arch Insect Biochem Physiol

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show abstract

“…The Benakeion mass rearing strain of C. capitata, having the standard gene arrangement (Zacharopoulou, 1990), was used in this study. This strain has been maintained in our laboratory for more than 30 years under standard conditions (25 ± 1°C, 40-50% relative humidity and 12 h light:12 h dark photoperiod) as previously described (Mintzas et al, 1983).…”

Section: Animals and Developmental Stagingmentioning

confidence: 99%

Cloning, characterization, and developmental expression of the ribosomal protein S21 gene of the Mediterranean fruit fly Ceratitis capitata

Verras

Theodoraki

Mintzas

2004

Arch Insect Biochem Physiol

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Ribosomal protein S21 (RpS21) belongs to a small group of ribosomal or ribosome-associated proteins. Mutations in the RpS21 gene cause dominant Minute and recessive lethal tumorous phenotypes in Drosophila melanogaster. Studies in several organisms suggest that RpS21 is involved in the regulation of protein synthesis and cell growth. In this report, we used an RT-PCR fragment of D. melanogaster RpS21 mRNA to clone a RpS21 cDNA from the Mediterranean fruit fly, Ceratitis capitata. The isolated cDNA contained both 5' and 3' untranslated regions, and encoded a polypeptide of 83 amino acids with a predicted molecular mass of 9.1 kDa. The deduced protein sequence showed 91% amino acid identity to D. melanogaster RpS21 and strong homology with all known ribosomal S21 proteins. DNA blot hybridization indicated the existence of a single RpS21 gene in the Ceratitis capitata genome. Analysis of the 5' untranslated region revealed the occurrence of a major oligopyrimidine tract at the 5' end, which characterizes most mRNAs undergoing a growth-dependent translational control. Study of the mRNA patterns during development suggested that the expression of Ceratitis RpS21 is temporally regulated at the level of transcription.

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“…The "ew dp," "B ap," and "Cu wp" strains were kindly supplied by Dr. Y. R6ssler (ROssler and Koltin, 1976;R6ssler, 1979 and1990). Moreover, the mutations "ew" and "dp" have been mapped at the third chromosome, the mutations "B" and "ap" at the fourth chromosome, and the mutations "Cu" and "wp" at the fifth chromosome (Malacrida et al, 1986;R6ssler, 1979;R6ssler and Rosenthal, 1990;Zacharopoulou, 1990).…”

Section: Strainsmentioning

confidence: 99%

Biochemical and genetic studies on alkaline phosphatase ofCeratitis capitata

1993

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Two forms of alkaline phosphatase exist in the integument of the "white pupae" (wp) and dark pupae (dp) mutant strains of Ceratitis capitata, during transition from larvae to pupae. They were separated by DEAE-cellulose chromatography. Both isoenzymes have a molecular weight of approximately 180,000 and two pH optima, at 9.4 and at 11.0. The isoenzymes of the "dark pupae" mutant catalyze the hydrolysis of phosphotyrosine and beta-glycerophosphate but not phosphoserine, phosphothreonine, ATP, and AMP. In contrast, the isoenzymes of the white pupae mutant hydrolyze all the substrates tested. The ALPase 1 of the dark pupae mutant was inhibited by L-tyrosine, but L-phenylalanine had no effect on either isoenzyme. The effects of divalent cations, EDTA, temperature, urea, and 2-mercaptoethanol were also investigated. Electrophoretic analysis did not reveal any variants of the larval and pupal isoenzymes, but ALPase A, an adult stage-specific isoenzyme, was found to be polymorphic. The electrophoretic variants were shown to be controlled by three codominant alleles located on the third chromosome of Ceratitis capitata. Since we found no hybrid enzyme, we conclude that ALPase A is monomeric.

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Polytene chromosome maps in the Medfly Ceratitis capitata

Cited by 85 publications

References 19 publications

cDNA cloning, characterization, and developmental expression of the 20S proteasome α5 subunit in the Mediterranean fruit fly Ceratitis capitata

cDNA cloning, characterization, and developmental expression of the 20S proteasome α5 subunit in the Mediterranean fruit fly Ceratitis capitata

Cloning, characterization, and developmental expression of the ribosomal protein S21 gene of the Mediterranean fruit fly Ceratitis capitata

Biochemical and genetic studies on alkaline phosphatase ofCeratitis capitata

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