DROSOPHILA RIBOSOMAL-PROTEIN S19 CDNA SEQUENCE
DROSOPHILA RIBOSOMAL-PROTEIN S19 CDNA SEQUENCE
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DOI:
10.1093/nar/21.16.3897
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发表时间:
1993-08-11
影响因子:
14.9
通讯作者:
CHIQUETEHRISMANN, R
中科院分区:
文献类型:
--
作者:
BAUMGARTNER, S;MARTIN, D;CHIQUETEHRISMANN, R
The eukaryotic ribosome is a complex structure consisting of 82 different proteins and 4 rRNA molecules. Sequence analysis of ribosomal proteins is essential for structural and functional studies and for understanding the evolution of ribosomes (1). Several ribosomal proteins from Drosophila have been described (2, 3, 4), some of which show interesting mutant phenotypes. For example, mutations in the Drosophila S6 gene cause enlargement and overproliferation of the hematopoietic organs (3, 4), thus, S6 can be considered a tumor suppressor gene. Many Minute (M) loci of Drosophila are thought to code for ribosomal proteins and mutations in these loci result in phenotypes indicative of reduced or slowed protein synthesis. These include prolonged larval development, etched tergites, tiin and short thoracic bristles, reduced fertility, a reduced rate of cell division and small cell size leading to reduced body size. Unlike in other eukaryotes (eg yeast, frog, mouse) the majority ofDrosophila ribosomal protein genes are single copy genes (2). We haveisolated a cDNA clone which apparently encodes Drosophila ribosomal protein S19 from a cDNA library constructed using poly A+ RNA from 0-16 h embryos. This cDNA consists of 22 nucleotides of 5'non coding sequence, a 471 nucleotide open reading frame, and 23 nucleotides of the 3'untranslated region (data not shown). As demonstrated by Northern analysis, the Drosophila S19 mRNA is approximately 700 bp in size, indicating that our cDNA is not a full length cDNA. The S19 mRNA is expressed abundantly in all life cycles (data not shown). Southern blot analysis ofDrosophila genomic DNA using the S19 cDNA as a probe shows a single band indicating that S19 is not part of a multigene family (data not shown).Analysis of the open reading frame of 156 amino acids revealed a 65% identity or 76% similarity (ifconservative changes were allowed) to the human and rat S19 ribosomal proteins (5, 6)(Figure 1). The Drosophila homologue contains a carboxyterminus extension which appears more highly diverged than other parts of the protein. The Drosophila S19 protein is 48% and 45% identical to the yeast (7) or Aspergillus nidulans (8) S16 proteins, which were shown to be the fungal homologues of the vertebrate S19proteins. Furthercomputer searches for proteins similar to Drosophila S19 recovered a putative ribosomal protein (ALEP-1) from Ascaris lumbricoides (9)(52% identity) which appears to be involved in the process of chromatin diminution.