Structural Analysis of a Developmentally Regulated 25-kDa Protein Gene of Sarcophaga peregrina1

Matsumoto, Noriko; Sekimizu, Kazuhisa; Soma, Gen‐Ichiro; Ohmura, Yoshihisa; Andoh, Toshiwo; Nakanishi, Yoshinobu; Obinata, Masuo; Natori, Shunji

doi:10.1093/oxfordjournals.jbchem.a135205

Cited by 18 publications

(11 citation statements)

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“…The sequence of six clones was determined using the dideoxy-chain termination method. Sequences were aligned to the Fbp2 cDNA sequence of D. melanogaster (Rat et al 1991) and S. peregrina (Matsumoto et al 1985).…”

Section: Methodsmentioning

confidence: 99%

“…Its amino acid similarity to ADH is low (28%), but the two proteins have retained structural homologies (Rat et al 1991). The sequence and the expression pattern of this gene are known in D. melanogaster and in Sarcophaga peregrina (Matsumoto et al 1985). Drosophila belongs to the acalyptrate Diptera, while Sarcophaga belongs to the calyptrate Diptera, along with the house fly.…”

Section: Introductionmentioning

confidence: 99%

“…If the start codon is excluded, there is no methionine in ADH. There are 51 methionines (20%) in D. melanogaster FBP2 (Rat et al 1991), and 29 (11.3%) in S. peregrina (Matsumoto et al 1985). Most of these methionines are at different positions in the two species.…”

Section: Introductionmentioning

confidence: 99%

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Selection and Methionine Accumulation in the Fat Body Protein 2 Gene (FBP2), a Duplicate of the Drosophila Alcohol Dehydrogenase (ADH) Gene

Meghlaoui

Veuille

1997

J Mol Evol

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The Drosophila fat body protein 2 gene (Fbp2) is an ancient duplication of the alcohol dehydrogenase gene (Adh) which encodes a protein that differs substantially from ADH in its methionine content. In D. melanogaster, there is one methionine in ADH, while there are 51 (20% of all amino acids) in FBP2. Methionine is involved in 46% of amino acid replacements when Fbp2 DNA sequences are compared between D. melanogaster and D. pseudoobscura. Methionine accumulation does not affect conserved residues of the ADH-ADHr-FBP2 multigene family. The multigene family has evolved by replacement of mildly hydrophobic amino acids by methionine with no apparent reversion. Its short-term evolution was compared between two Drosophila species, while its long-term evolution was compared between two genera belonging respectively to acalyptrate and calyptrate Diptera, Drosophila and Sarcophaga. The pattern of nucleotide substitution was consistent with an independent accumulation of methionines at the Fbp2 locus in each lineage. Under a steady-state model, the rate of methionine accumulation was constant in the lineage leading to Drosophila, and was twice as fast as that in the calyptrate lineage. Substitution rates were consistent with a slight positive selective advantage for each methionine change in about one-half of amino acid sites in Drosophila. This shows that selection can potentially account for a large proportion of amino acid replacements in the molecular evolution of proteins.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Selection and Methionine Accumulation in the Fat Body Protein 2 Gene (FBP2), a Duplicate of the Drosophila Alcohol Dehydrogenase (ADH) Gene

Meghlaoui

Veuille

1997

J Mol Evol

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“…As controls of other fat-body protein genes, pT019 [ 1 I] and pTII20 [I 21, cDNA clones for sarcotoxin IA and IIA (antibacterial proteins of Sarcophaga), respectively, and pS25 [13], a genomic clone for 25-kDa protein, were used.…”

Section: Northern Blot Hybridizationmentioning

confidence: 99%

A novel mechanism of Sarcophaga lectin gene expression

Sugiyama

Natori

1991

European Journal of Biochemistry

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The Sarcophaga lectin gene, an acute‐phase‐responsive protein of Sarcophaga, was found to be activated when the fat body was incubated in phosphate‐buffered insect saline (10 mM NaH2PO4/Na2HPO4, pH 6.2, 2 mM NaHCO3, 1 mM MgCl2, 5 mM KCl, 1 mM CaCl2 and 120 mM NaCl). This activation was selectively suppressed by addition of 2‐mercaptoethanol. 2‐Mercaptoethanol did not affect the transcription directly, suggesting that the oxidation of the sulfhydryl group of a fat‐body protein is required for activation of the Sarcophaga lectin gene. This oxidation reaction seemed to occur immediately when the fat body was incubated in vitro, and once this reaction was initiated, 2‐mercaptoethanol no longer inhibited transcription of the Sarcophaga lectin gene. This gene is known to be activated when the larval‐body wall of Sarcophaga is injured. It is suggested that the Sarcophaga lectin gene is activated via this novel mechanism on its acute‐phase expression in vivo.

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“…3. This motif was found in the defense protein genes but not in the arylphorin gene (25) the 25-kDa protein (alcohol dehydrogenase homolog) gene of S. peregrina (27).…”

mentioning

confidence: 93%

Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).

Kobayashi¹,

Matsui²,

Kubo³

et al. 1993

Mol. Cell. Biol.

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Various Sarcophaga peregrina (flesh fly) defense protein genes were shown to be activated when NIH-Sape-4 cells were cultured with bacterial lipopolysaccharides or 0-1,3-glucan. The 5' upstream regions of the defense protein genes were found to have common motifs showing similarity to the mammalian NF-KB-binding consensus sequence. A protein with affinity to the NF-KB-binding motif of the Sarcophaga lectin promoter was identified and purified to near homogeneity. This 59-kDa protein also bound to the NF-KB-binding motifs of other defense protein genes, e.g., sarcotoxin I and sarcotoxin II genes. This protein was found in both the cytoplasmic and the nuclear fractions of the cells, and it appeared to migrate from the cytoplasm to the nucleus on treatment of the cells with lipopolysaccharides. This 59-kDa protein is probably a transcriptional regulator of the genes for defense proteins of S. peregnna.

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Structural Analysis of a Developmentally Regulated 25-kDa Protein Gene of Sarcophaga peregrina1

Cited by 18 publications

References 0 publications

Selection and Methionine Accumulation in the Fat Body Protein 2 Gene (FBP2), a Duplicate of the Drosophila Alcohol Dehydrogenase (ADH) Gene

Selection and Methionine Accumulation in the Fat Body Protein 2 Gene (FBP2), a Duplicate of the Drosophila Alcohol Dehydrogenase (ADH) Gene

A novel mechanism of Sarcophaga lectin gene expression

Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).

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