Identification and developmental expression of a 5'-3' exoribonuclease from Drosophila melanogaster. 1998

D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
Biophysics Laboratories, School of Biological Sciences, University of Portsmouth, UK.

In multicellular organisms, very little is known about the role of mRNA stability in development, and few proteins involved in degradation pathways have been characterized. We have identified the Drosophila homologue of XRN1, which is the major cytoplasmic 5'-3' exoribonuclease in Saccharomyces cerevisiae. The protein sequence of this homologue (pacman) has 59% identity to S. cerevisiae XRN1 and 67% identity to the mouse homologue (mXRN1p) in certain regions. Sequencing of this cDNA revealed that it includes a trinucleotide repeat (CAG)9 which encodes polyglutamine. By directly measuring pacman exoribonuclease activity in yeast, we demonstrate that pacman can complement the yeast XRN1 mutation. Northern blots show a single transcript of approximately 5.2 kb which is abundant only in 0-8-h embryos and in adult males and females. In situ hybridization analysis revealed that the pcm transcripts are maternally derived, and are expressed at high levels in nurse cells. During early embryonic syncytial nuclear divisions, pcm transcripts are homogenously distributed. pcm mRNA is expressed abundantly and ubiquitously throughout the embryo during gastrulation, with high levels in the germ band and head structures. After germ band retraction, pcm transcripts are present at much lower levels, in agreement with the Northern results. Our experiments provide the first example of an exoribonuclease which is differentially expressed throughout development.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D009865 Oocytes Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM). Ovocytes,Oocyte,Ovocyte
D011061 Poly A A group of adenine ribonucleotides in which the phosphate residues of each adenine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Adenine Polynucleotides,Polyadenylic Acids,Poly(rA),Polynucleotides, Adenine
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004331 Drosophila melanogaster A species of fruit fly frequently used in genetics because of the large size of its chromosomes. D. melanogaster,Drosophila melanogasters,melanogaster, Drosophila
D005095 Exoribonucleases A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.- Exoribonuclease
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015003 Yeasts A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED. Yeast

Related Publications

D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
January 2001, Methods in enzymology,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
April 1998, Gene,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
January 2001, Methods in enzymology,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
December 1997, Nucleic acids research,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
January 1989, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
August 2005, American journal of physiology. Cell physiology,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
May 2024, Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
July 2000, The Journal of biological chemistry,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
January 2015, RNA biology,
D D Till, and B Linz, and J E Seago, and S J Elgar, and P E Marujo, and M L Elias, and C M Arraiano, and J A McClellan, and J E McCarthy, and S F Newbury
September 1992, The International journal of developmental biology,
Copied contents to your clipboard!