Regulation of tubulin gene expression during embryogenesis in drosophila melanogaster

Raff, Elizabeth C.; Fuller, Margaret T.; Kaufman, Thomas C.; Kemphues, Kenneth J.; Rudolph, J; Raff, Rudolf A.

doi:10.1016/0092-8674(82)90372-5

Cell

1982

DOI: 10.1016/0092-8674(82)90372-5

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Regulation of tubulin gene expression during embryogenesis in drosophila melanogaster

Elizabeth C. Raff

Margaret T. Fuller

Thomas C. Kaufman

et al.

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Cited by 79 publications

(28 citation statements)

References 34 publications

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“…The proteins encoded by these genes constitute distinct sequence types which are considerably divergent from each other, exhibiting only 87% homology in overall amino acid sequence. The sequence differences between the two isoforms confirm the differences we observed previously in electrophoretic properties of the two isoforms (20,50 82 GO GAT GAG GAG GOC GAA TTC GAT GAA GAGAA GAG GOT GOC GOC GAT GAA TM TAG Ala Asp Glu Glu Gly Glu Phe Asp Glu Asp Glu Glu Gly Gly Gly Asp Glu -- The single intron of the ,2-tubulin gene and the corresponding third intron of the 133-tubulin gene are similar in size but do not exhibit a significant degree of sequence homology. The conserved 3' and 5' consensus sites required for eucaryotic message processing are indicated for each of the introns (7,38 are compared with a number of other beta-tubulins in Fig.…”

supporting

confidence: 79%

“…That is, ,B3-tubulin is also divided into a carboxyl alpha-helical region and an amino-terminal beta-sheet domain, and the specific regions of predicted secondary structure are homologous between the two proteins. The additional amino acids present in 13-tubulin at the second intron junction fall into a region of the molecule of uncertain structure (see the region at amino acids 50 to 75 in the model for ,B2-tubulin in Fig. 6).…”

mentioning

confidence: 99%

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Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function.

Rudolph¹,

Kimble²,

Hoyle³

et al. 1987

Mol. Cell. Biol.

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The genomic DNA sequence and deduced amino acid sequence are presented for three Drosophila melanogaster beta-tubulins: a developmentally regulated isoform ,3-tubulin, the wild-type testis-specific isoform 132-tubulin, and an ethyl methanesulfonate-induced assembly-defective mutation of the testis isoform, B218. The testis-specific j2-tubulin is highly homologous to the major vertebrate beta-tubulins, but j3-tubulin is considerably diverged. Comparison of the amino acid sequences of the two Drosophila isoforms to those of other beta-tubulins indicates that these two proteins are representative of an ancient sequence divergence event which at least preceded the split between lines leading to vertebrates and invertebrates. The intron/exon structures of the genes for 02-and 03-tubulin are not the satne. The structure of the gene for the variant ,3-tubulin isoform, but not that of the testis-specific 112-tubulin gene, is similar to that of vertebrate beta-tubulins. The mutation B218 in the gene for the testis-specific ,2-tubulin defines a single amino acid residue required for normal assembly function of beta-tubulin. The sequence of the B218 gene is identical to that of the wild-type gene except for a single nucleotide change resulting in the substitution of lysine for glutamic acid at residue 288. This position falls at the junction between two major structural domains of the beta-tubulin molecule. Although this hinge region is relatively variable in sequence among different beta-tubulins, the residue corresponding to glu 288 of Drosophila 12-tubulin is highly conserved as an acidic amino acid not only in all other beta-tubulins but in alpha-tubulins as well.

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supporting

confidence: 79%

mentioning

confidence: 99%

Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function.

Rudolph¹,

Kimble²,

Hoyle³

et al. 1987

Mol. Cell. Biol.

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“…In some cases, the presence of multiple genes may have allowed the evolution of specialized control mechanisms for individual genes in the family. In multi-cellular organisms, including Drosophila melanogaster and chickens and rats, the various tubulin genes exhibit tissue-specific or developmental stage-specific expression (5,15,28,40). In the slime mold Physarum polycephalum, plasmodium-specific expression of one a-and one ,B-tubulin gene has been observed (8).…”

mentioning

confidence: 99%

The two beta-tubulin genes of Chlamydomonas reinhardtii code for identical proteins.

1984

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The two "-tubulin genes of the unicellular green alga Chiamydomonas reinhardtii are expressed coordinately after deflagellation and produce two transcripts of 2.1 and 2.0 kiobases. Full-length cDNA clones corresponding to the transcript of each gene were isolated. DNA sequences were obtained from the cDNA clones and from cloned tubulin gene fragments. Both genes contained 1,332 base pairs of coding sequence, with only 19 nucleotide differences between the genes. Because all the differences occurred at the third base position of a codon and did not change the predicted amino acid sequence, we concluded that both 0-tubulin genes code for the same protein of 443 amino acids. The predicted amino acid sequence is 89 and 72% homologous with Dtubulins from chicken and yeast cells, respectively. Each gene had three intervening sequences, which occurred at identical positions. Although the first two intervening sequences were not conserved between the two genes, the nucleotide sequence of the third intervening sequence was 89% conserved between the genes. The codon usage in the tubulin genes of C. reinhardhii was very biased: only 37 different codons were used. Striking differences occurred between the codons used in these nuclear genes and C. reinhardtii chloroplast genes.

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“…families are differentially expressed during embryonic development and in different adult tissues (21,23,31,35). However, little is known about the regulation of synthesis of these proteins during murine embryogenesis, though changes in protein synthesis have been demonstrated (17) to occur during early embryonic development.…”

mentioning

confidence: 99%

Post-transcriptional regulation of the abundance of mRNAs encoding alpha-tubulin and a 94,000-dalton protein in teratocarcinoma-derived stem cells versus differentiated cells.

Howe¹,

Lugg²,

Overton³

1984

Mol. Cell. Biol.

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Changes in the expression of the genes encoding a-tubulin and a 94,000-dalton protein (p94) specified by a cDNA clone, p4-30, were examined in a differentiated teratocarcinoma-derived parietal endoderm cell line, PYS-2, and an undifferentiated teratocarcinoma stem cell line, F9. Relative to other proteins or mRNA species, the synthesis rate of the a-tubulins and of p94, as well as the levels of their corresponding cytoplasmic mRNAs, were lower in PYS-2 than in F9 cells. The decrease was greater for the relative abundance of cytoplasmic a-tubulin mRNA than for p94 mRNA. Similarly, induction of differentiation of F9 cells by simultaneous exposure to retinoic acid (RA) and dibutyryl cyclic AMP resulted in reduced relative levels of the cytoplasmic mRNAs for these proteins. The reduction in abundance of the two RNA species was not due to a decrease in growth rate since the differentiated cells, PYS-2, RA-treated F9, and RA plus dibutyryl cyclic AMP-treated F9 cells, grew at a rate similar to that of undifferentiated F9 cells. However, induction of differentiation of F9 cells by treatment with RA alone did not cause down-regulation of the two RNA species. The relative levels of total cellular RNA encoding ca-tubulin and p94 in PYS-2 cells were also lower than those in F9 cells to an extent comparable to the decrease in the cytoplasmic RNAs. Since the apparent relative rates of RNA transcription were similar in both cell types, we conclude that the reduction in relative levels of the a-tubulin and p94 RNAs in the cell depends largely on the relative stability of the two RNAs and not on the relative rates of transcription. The faster disappearance of the two RNA species relative to other cellular RNAs from actinomycin D-treated PYS-2 compared with F9 cells is consistent with this interpretation.Microtubules consist of two proteins, a-and ,B-tubulin, each shown in human, chicken, and Drosophila melanogaster to contain several distinct genes (7,8,10,20,37,46). In D. melanogaster, members of the a-and P-tubulin multigene families are differentially expressed during embryonic development and in different adult tissues (21,23,31,35). However, little is known about the regulation of synthesis of these proteins during murine embryogenesis, though changes in protein synthesis have been demonstrated (17) to occur during early embryonic development. A recent study (9) showed that treatment of Chinese hamster ovary cells with the microtubule-depolymerizing drug colchicine resulted in the specific and rapid loss of tubulin mRNA from the cytoplasm. It was suggested that this loss of tubulin mRNA was probably not achieved through a transcriptionally regulated mechanism since the relative rates of tubulin RNA transcription are essentially unchanged in isolated nuclei derived from colchicine-treated and untreated control cells (6). In contrast, expression of globin genes in a hemintreated human erythroid cell line (5) and of a-fetoprotein and albumin genes in liver from late prenatal to 1-month-postpartum mice (43) is regulated primar...

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Regulation of tubulin gene expression during embryogenesis in drosophila melanogaster

Cited by 79 publications

References 34 publications

The two beta-tubulin genes of Chlamydomonas reinhardtii code for identical proteins.

Post-transcriptional regulation of the abundance of mRNAs encoding alpha-tubulin and a 94,000-dalton protein in teratocarcinoma-derived stem cells versus differentiated cells.

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