Identification and characterization of the gene for Drosophila S20 ribosomal protein (original) (raw)
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Biochimica Et Biophysica Acta-gene Structure and Expression, 1994
We describe the cDNA sequence of the Drosophila homologue of the rat ribosomal protein L18a. The protein sequence predicted has identical or conservatively substituted amino acids in 80% of positions. It is distinctly basic in character with an overall net positive charge of + 20. Analysis of L18a RNA with the Northern blot technique shows it to be expressed both during embryonic development and in the adult fly. In situ hybridisation to polytene chromosomes reveals that the L18a gene(s) is located at 54B on the second chromosome.
Molecular and cellular biology, 1988
We describe a Drosophila DNA clone of tandemly duplicated genes encoding an amino acid sequence nearly identical to human ribosomal protein S14 and yeast rp59. Despite their remarkably similar exons, the locations and sizes of introns differ radically among the Drosophila, human, and yeast (Saccharomyces cerevisiae) ribosomal protein genes. Transcripts of both Drosophila RPS14 genes were detected in embryonic and adult tissues and are the same length as mammalian S14 message. Drosophila RPS14 was mapped to region 7C5-9 on the X chromosome. This interval also encodes a previously characterized Minute locus, M(1)7C.
The ribosomal protein genes and Minute loci of Drosophila melanogaster
Genome biology, 2007
Mutations in genes encoding ribosomal proteins (RPs) have been shown to cause an array of cellular and developmental defects in a variety of organisms. In Drosophila melanogaster, disruption of RP genes can result in the 'Minute' syndrome of dominant, haploinsufficient phenotypes, which include prolonged development, short and thin bristles, and poor fertility and viability. While more than 50 Minute loci have been defined genetically, only 15 have so far been characterized molecularly and shown to correspond to RP genes. We combined bioinformatic and genetic approaches to conduct a systematic analysis of the relationship between RP genes and Minute loci. First, we identified 88 genes encoding 79 different cytoplasmic RPs (CRPs) and 75 genes encoding distinct mitochondrial RPs (MRPs). Interestingly, nine CRP genes are present as duplicates and, while all appear to be functional, one member of each gene pair has relatively limited expression. Next, we defined 65 discrete Minu...
The Drosophila homologue of ribosomal protein L8
Insect Biochemistry and Molecular Biology, 1999
We have cloned the gene encoding the Drosophila melanogaster homologue of ribosomal protein L8. It contains two introns: one in the 5Ј untranslated region and the second in the beginning of the ORF, and encodes a 256-residue protein which is highly conserved when compared with RpL8 proteins of other organisms. The gene is present as a single copy in the Drosophila genome and maps at position 62E6-7 on polytene chromosomes. It is expressed ubiquitously at all stages of development. It is located close to the gene encoding RpL12 and both are candidate targets of the Minute mutation, M(3)LS2, mapped in the region 62E-63A.
The Drosophila melanogaster ribosomal protein L17A-encoding gene
Gene, 1992
The structure and sequence of the gene encoding the Drosophila melanogaster homolog of the human and yeast largesubunit ribosomal protein L17A (rpL17A) is presented. The deduced amino acid (aa) sequence of 140 residues exhibits 870/, and 77% identity to that of the human (140 aa) and yeast (137 aa) rpL17As, respectively. The D. melanogaster rpLl7A gene is single copy and maps at 58F6-59A3, a chromosome region encompassing a previously characterized Minute locus, h4(2)1. Despite this extensive homology in their protein products, the D. melanogaster and yeast rpLl7A genes display different exon-intron structures, with the first D. melanogaster intron mapping within the 5'-untranslated mRNA leader. The rpLl7A gene gives rise to a single 600-nucleotide transcript present throughout development, and is located close to another similarly expressed gene. The 5' end of the D. melanogaster rpLl7A mRNA contains a polypyrimidine tract displayed by several mammalian rp genes and involved in translational control of their expression.
Nucleic Acids Research, 2011
Several ribosomal protein families contain paralogues whose roles may be equivalent or specialized to include extra-ribosomal functions. RpL22e family members rpL22 and rpL22-like are differentially expressed in Drosophila melanogaster: rpL22-like mRNA is gonad specific whereas rpL22 is expressed ubiquitously, suggesting distinctive paralogue functions. To determine if RpL22-like has a divergent role in gonads, rpL22-like expression was analysed by qRT-PCR and western blots, respectively, showing enrichment of rpL22-like mRNA and a 34 kDa (predicted) protein in testis, but not in ovary. Immunohistochemistry of the reproductive tract corroborated testis-specific expression. RpL22-like detection in 80S/polysome fractions from males establishes a role for this tissue-specific paralogue as a ribosomal component. Unpredictably, expression profiles revealed a low abundant, alternative mRNA variant (designated 'rpL22-like short') that would encode a novel protein lacking the C-terminal ribosomal protein signature but retaining part of the N-terminal domain. This variant results from splicing of a retained intron (defined by non-canonical splice sites) within rpL22-like mRNA. Polysome association and detection of a low abundant 13.5 kDa (predicted) protein in testis extracts suggests variant mRNA translation. Collectively, our data show that alternative splicing of rpL22-like generates structurally distinct protein products: ribosomal component RpL22-like and a novel protein with a role distinct from RpL22-like.
Nucleic Acids Research, 2000
The expression of ribosomal protein (r-protein) genes is uniquely regulated at the translational level during early development of Drosophila. Here we report results of a detailed analysis of the r-protein rpAl gene. A cloned DNA sequence coding for rpAl has been identified by hybrid-selected translation and amino acid composition analysis. The rpAl gene was localized to polytene chromosome band 53CD.
minifly, A Drosophila Gene Required for Ribosome Biogenesis
The Journal of Cell Biology, 1999
We report here the genetic, molecular, and functional characterization of the Drosophila melanogaster minifly ( mfl ) gene. Genetic analysis shows that mfl is essential for Drosophila viability and fertility. While P-element induced total loss-of-function mutations cause lethality, mfl partial loss-of-function mutations cause pleiotropic defects, such as extreme reduction of body size, developmental delay, hatched abdominal cuticle, and reduced female fertility. Morphological abnormalities characteristic of apoptosis are found in the ovaries, and a proportion of eggs laid by mfl mutant females degenerates during embryogenesis. We show that mfl encodes an ubiquitous nucleolar protein that plays a central role in ribosomal RNA process-ing and pseudouridylation, whose known eukaryotic homologues are yeast Cfb5p, rat NAP57 and human dyskerin, encoded by the gene responsible for the X-linked dyskeratosis congenita disease. mfl genetic analysis represents the first in vivo functional characterization of a member of this highly conserved gene family from higher eukaryotes. In addition, we report that mfl hosts an intron encoded box H/ACA snoRNA gene, the first member of this class of snoRNAs identified so far from Drosophila .