Sequence and structure of the dopa decarboxylase gene of Drosophila: evidence for novel RNA splicing variants.

Eveleth, D D; Gietz, R. Daniel; Spencer, Charlotte A.; Nargang, Frank E.; Hodgetts, Ross B.; Marsh, J. Lawrence

doi:10.1002/j.1460-2075.1986.tb04549.x

Cited by 115 publications

(71 citation statements)

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“…It seems that TDC, too, has a site particularly susceptible to proteolysis and located about two-thirds from the N-terminus. By comparing the amino acid sequence for the N-terminus of the 14 kDa fragment [14] with the sequences for TDC from C. roseus [15] and for dopa decarboxylase from Drosophila melanogaster [ 16,17], it can be deduced that the site of proteolytic cleavage might be lysine-350 of TDC. Cleavage at this site would yield fragments with calculated Mr values of 38 735 and 17 489.…”

Section: Resultsmentioning

confidence: 99%

Tryptophan decarboxylase from Catharanthus roseus is a pyridoxoquinoprotein

et al. 1989

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Tryptophan decarboxylase (EC 4.1.1.28) from Catharanthus roseus was purified to homogeneity. The native enzyme has an M r of about 96000 as estimated from native PAGE. After SDS‐PAGE, three protein bands were visible corresponding with M r 49000, 33000 and 17000. The N‐termini of the 49 kDa protein and the 33 kDa protein were identical. Antibodies against the 49 kDA protein also reacted strongly with the two smaller proteins. It is concluded that the native enzyme consists of two subunits of M r 49000. Tryptophan decarboxylase appears to be a pyridoxo‐quinoprotein, since two molecules of pyridoxal phosphate and two molecules of covalently‐bound pyrroloquinoline quinone were found per enzyme molecule.

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Section: Resultsmentioning

confidence: 99%

Tryptophan decarboxylase from Catharanthus roseus is a pyridoxoquinoprotein

et al. 1989

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“…A recombinant phage isolated from the same genomic library that contained the lethal(2)giant larvae (l[2]gl) gene (C. Segarra and M. Aguadé, unpubl. data) was also used as well as four clones from D. melanogaster with a known genic content: numb (Uemura et al 1989), dopa decarboxilase (Ddc; Eveleth et al 1986), Myosin heavy chain (Mhc; Berstein et al 1983), and Histone (His; Matsuo and Yamasaki 1989). Finally, the hybridization site of the Alcohol dehydrogenase (Adh) gene in the three species was obtained from the literature (Goldberg 1980;Schaeffer and Aquadro 1987;Visa et al 1991).…”

Section: Methodsmentioning

confidence: 99%

Chromosomal Evolution of Elements B and C in the Sophophora Subgenus of Drosophila: Evolutionary Rate and Polymorphism

2006

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Abstract. The locations of 77 markers along the chromosomal elements B (41 markers) and C (36 markers) of Drosophila subobscura, D. pseudoobscura, and D. melanogaster were obtained by in situ hybridization on polytene chromosomes. In comparisons between D. subobscura and D. pseudoobscura, 10 conserved segments (accounting for 32% of the chromosomal length) were detected on element B and eight (17% of the chromosomal length) on element C. The fixation rate of paracentric inversions inferred by a maximum likelihood approach differs significantly between elements. Muller's element C (0.17 breakpoints/Mb/million years) is evolving two times faster than element B (0.08 breakpoints/Mb/million years). This difference in the evolutionary rate is paralleled by differences in the extent of chromosomal polymorphism in the corresponding lineages. Element C is highly polymorphic in D. subobscura, D. pseudoobscura, and in other obscura group species such as D. obscura and D. athabasca. In contrast, the level of polymorphism in element B is much lower in these species. The fixation rates of paracentric inversions estimated in the present study between species of the Sophophora subgenus are the highest estimates so far reported in the genus for the autosomes. At the subgenus level, there is also a parallelism between the high fixation rate and the classical observation that the species of the Sophophora subgenus tend to be more polymorphic than the species of the Drosophila subgenus. Therefore, the detected relationship between level of polymorphism and evolutionary rate might be a general characteristic of chromosomal evolution in the genus Drosophila.Key words. Chromosomal elements, chromosomal evolution, chromosomal inversions, chromosomal polymorphism, Drosophila, Drosophila obscura group, evolutionary rate. The comparative analysis of chromosomal organization, mainly synteny and gene order, has been the focus of recent studies on chromosomal evolution. Changes in gene order are due to rearrangements affecting either small or large chromosomal segments (micro-or macro-rearrangements). After the sequencing of the whole genome of several organisms, both prokaryotes and eukaryotes, the analysis of gene order conservation is possible by direct comparison of complete genome sequences. The first genomewide comparative studies were performed between quite distant bacterial genomes and suggested a rapid evolution of gene order Tatusov et al. 1996). Later studies revealed that in yeast gene order evolution has been mainly shaped by small inversions including fewer than 10 genes (Seoighe et al. 2000). In eukaryotes with more complex genomes, the genomewide comparative studies have been extremely useful to detect groups of genes with conserved synteny, for instance, between humans and mouse (Kent et al. 2003;Pevner and Tesler 2003) or between Drosophila melanogaster and D. pseudoobscura (Richards et al. 2005).At another scale, the genome projects have facilitated the comparative mapping of multiple markers by in situ hybridization, es...

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“…The putative seven-amino acid pyridoxal phosphate (PLP)-binding domain (amino acids 307-313) and the PLP-binding site (Lys-312) are completely identical in both the cDNA and amino acid sequences, respectively, in P-815 cells and rat liver. Interestingly, the threonine-307 and serine-311 residues of HDC are replaced by asparagine and histidine residues, respectively, in rat [12] and Drosophila DDC [13]. Although the significance of these differences in this domain is unclear, it is possible that the amino acid sequence surrounding the PLP-binding site (lysine) may be substrate-specific.…”

Section: S-mentioning

confidence: 99%

cDNA‐derived amino acid sequence of L‐histidine decarboxylase from mouse mastocytoma P‐815 cells

et al. 1990

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The primary structure of L-hi&dine decarboxylase (HDC: L-histidine carboxy-lyase, EC 4.1.1.22) from mouse mastocytoma P-81 5 cells has been determined by parallel analysis of the amino acid sequence of the protein and the nucleotide sequence of the corresponding cDNA. HDC contains 662 amino acid residues with a molecular mass of 74 017, which is larger by about 21000 Da than that of the previously purified HDC subunit (53 kDa), suggesting that HDC might be posttranslationally processed. The HDC cDNA hybridized to a 2.7 kilobase mRNA of mastocytoma cells. Homology was found between the sequences of mouse mastocytoma HDC and fetal rat liver HDC.Histidine decarboxylase; Mastocytoma P-8 15 cell; Amino acid sequence; cDNA sequence; Dopa decarboxylase; Polymerase chain reaction

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Sequence and structure of the dopa decarboxylase gene of Drosophila: evidence for novel RNA splicing variants.

Cited by 115 publications

References 50 publications

Tryptophan decarboxylase from Catharanthus roseus is a pyridoxoquinoprotein

Tryptophan decarboxylase from Catharanthus roseus is a pyridoxoquinoprotein

Chromosomal Evolution of Elements B and C in the Sophophora Subgenus of Drosophila: Evolutionary Rate and Polymorphism

cDNA‐derived amino acid sequence of L‐histidine decarboxylase from mouse mastocytoma P‐815 cells

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