scholarly journals Characterization and developmental expression of a Drosophila ras oncogene.

1985 ◽  
Vol 5 (4) ◽  
pp. 885-889 ◽  
Author(s):  
B Mozer ◽  
R Marlor ◽  
S Parkhurst ◽  
V Corces
Keyword(s):  
Developmental Expression ◽  
Ras Oncogene ◽  
Coding Region ◽  
Ras Gene ◽  
Amino Acid Homology ◽  
Ras Genes ◽  
Human Counterpart ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma

We cloned a Drosophila melanogaster ras gene (Dmras64B) on the basis of its homology to the ras oncogen from Harvey murine sarcoma virus. This gene mapped at chromosomal position 64B on the left arm of the third chromosome. Sequencing of Dmras64B revealed extensive amino acid homology with the proteins encoded by the human and Saccharomyces cerevisiae ras genes. The coding region of the Drosophila gene is interrupted by two introns located in different positions with respect to its human counterpart. Dmras64B encodes three different RNAs (1.6, 2.1, and 2.6 kilobases long) that are constantly expressed throughout the development of the fly.

Characterization and developmental expression of a Drosophila ras oncogene

1985 ◽  
Vol 5 (4) ◽  
pp. 885-889
Author(s):  
B Mozer ◽  
R Marlor ◽  
S Parkhurst ◽  
V Corces
Keyword(s):  
Developmental Expression ◽  
Ras Oncogene ◽  
Coding Region ◽  
Ras Gene ◽  
Amino Acid Homology ◽  
Ras Genes ◽  
Human Counterpart ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma

We cloned a Drosophila melanogaster ras gene (Dmras64B) on the basis of its homology to the ras oncogen from Harvey murine sarcoma virus. This gene mapped at chromosomal position 64B on the left arm of the third chromosome. Sequencing of Dmras64B revealed extensive amino acid homology with the proteins encoded by the human and Saccharomyces cerevisiae ras genes. The coding region of the Drosophila gene is interrupted by two introns located in different positions with respect to its human counterpart. Dmras64B encodes three different RNAs (1.6, 2.1, and 2.6 kilobases long) that are constantly expressed throughout the development of the fly.

scholarly journals Nucleotide sequence of the two rat cellular rasH genes.

1986 ◽  
Vol 6 (5) ◽  
pp. 1706-1710 ◽  
Author(s):  
M Ruta ◽  
R Wolford ◽  
R Dhar ◽  
D Defeo-Jones ◽  
R W Ellis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Coding Region ◽  
3T3 Cells ◽  
Ras Gene ◽  
P21 Protein ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Nih 3T3 ◽  
Murine Sarcoma

We present the nucleotide sequence of the coding region of the rat c-rasH-1 gene and a partial sequence analysis of the rat c-rasH-2 gene. By comparing these sequences with the Harvey murine sarcoma virus ras gene, we predict that the p21 protein encoded by the Harvey virus differs from the cellular c-rasH-1-encoded p21 at only two amino acids; those at positions 12 and 59. Alterations at each of these positions may play a role in activating the viral p21 protein. The c-rasH-2 gene is likely to be a nonfunctional pseudogene because it lacks introns, cannot be activated to transform NIH 3T3 cells, and differs in sequence from both c-rasH-1 and v-rasH at several base pair positions.

scholarly journals Presence of a Kirsten murine sarcoma virus ras oncogene in cells transformed by 3-methylcholanthrene.

1983 ◽  
Vol 3 (12) ◽  
pp. 2298-2301 ◽  
Author(s):  
L F Parada ◽  
R A Weinberg
Keyword(s):  
Human Tumor ◽  
Mouse Fibroblast ◽  
Ras Oncogene ◽  
Ras Gene ◽  
In Vitro Exposure ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma ◽  
In Cells

Oncogenes have previously been reported in the DNAs of mouse fibroblast lines which had become transformed after in vitro exposure to the carcinogen 3-methylcholanthrene. These oncogenes are now shown to be versions of the cellular Kirsten ras gene and are therefore homologous to oncogenes detected in a variety of human tumor DNAs.

Presence of a Kirsten murine sarcoma virus ras oncogene in cells transformed by 3-methylcholanthrene

1983 ◽  
Vol 3 (12) ◽  
pp. 2298-2301
Author(s):  
L F Parada ◽  
R A Weinberg
Keyword(s):  
Human Tumor ◽  
Mouse Fibroblast ◽  
Ras Oncogene ◽  
Ras Gene ◽  
In Vitro Exposure ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma ◽  
In Cells

Oncogenes have previously been reported in the DNAs of mouse fibroblast lines which had become transformed after in vitro exposure to the carcinogen 3-methylcholanthrene. These oncogenes are now shown to be versions of the cellular Kirsten ras gene and are therefore homologous to oncogenes detected in a variety of human tumor DNAs.

Nucleotide sequence of the two rat cellular rasH genes

1986 ◽  
Vol 6 (5) ◽  
pp. 1706-1710
Author(s):  
M Ruta ◽  
R Wolford ◽  
R Dhar ◽  
D Defeo-Jones ◽  
R W Ellis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Coding Region ◽  
3T3 Cells ◽  
Ras Gene ◽  
P21 Protein ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Nih 3T3 ◽  
Murine Sarcoma

We present the nucleotide sequence of the coding region of the rat c-rasH-1 gene and a partial sequence analysis of the rat c-rasH-2 gene. By comparing these sequences with the Harvey murine sarcoma virus ras gene, we predict that the p21 protein encoded by the Harvey virus differs from the cellular c-rasH-1-encoded p21 at only two amino acids; those at positions 12 and 59. Alterations at each of these positions may play a role in activating the viral p21 protein. The c-rasH-2 gene is likely to be a nonfunctional pseudogene because it lacks introns, cannot be activated to transform NIH 3T3 cells, and differs in sequence from both c-rasH-1 and v-rasH at several base pair positions.

scholarly journals Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs.

1984 ◽  
Vol 4 (8) ◽  
pp. 1647-1652 ◽  
Author(s):  
L S Ulsh ◽  
T Y Shih
Keyword(s):  
Bladder Carcinoma ◽  
Half Life ◽  
P21 Protein ◽  
Metabolic Turnover ◽  
Ras Genes ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Processed Products ◽  
Murine Sarcoma ◽  
P21 Proteins

The EJ bladder carcinoma oncogene is activated by a point mutation in the c-rasH proto-oncogene at the 12th amino acid codon. In an attempt to understand the mechanism of oncogenic activation, a comparative study was undertaken to examine the metabolic turnover and subcellular localization of the p21 protein encoded by the EJ oncogene, the viral oncogene, and its normal cellular homolog. Pulse-labeling experiments indicated that both c-ras p21 proteins were synthesized by a very similar pathway, as was observed for the viral p21 protein of Harvey murine sarcoma virus. The pro-p21 proteins were detected in free cytosol, and the processed products were associated with plasma membrane. The intracellular half-life of p21 proteins was determined by pulse-labeling and chasing in the presence of excess unlabeled methionine. Although both p21 proteins of EJ and the normal c-ras genes which are not phosphorylated have a half-life of 20 h, the viral p21 protein of Harvey murine sarcoma virus which includes a phosphorylated form is much more stable in cells, having a half-life of 42 h, apparently due to phosphorylation.

Mouse cells contain two distinct ras gene mRNA species that can be translated into a p21 onc protein

1982 ◽  
Vol 2 (11) ◽  
pp. 1339-1345
Author(s):  
R W Ellis ◽  
D DeFeo ◽  
M E Furth ◽  
E M Scolnick
Keyword(s):  
Normal Mouse ◽  
Velocity Sedimentation ◽  
Ras Gene ◽  
Mrna Species ◽  
P21 Ras ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Mouse Cells ◽  
Murine Sarcoma

The Kirsten (Ki) and Harvey (Ha) strains of murine sarcoma virus encode a 21,000-dalton protein (p21 ras) which is the product of the transforming gene of these viruses. Normal cells express low levels of p21 ras encoded by cellular genes (Ki-ras and Ha-ras) homologous to the Ki and Ha murine sarcoma virus transformation genes. A bone marrow-derived mouse cell line, 416B, has been shown to express unusually high levels of p21 ras. In this manuscript, we investigated the molecular biology of p21 ras gene expression in 416B and other normal mouse cells. We identified four distinct polyadenylated and polysome-associated RNAs, two related to Ki-ras and two to Ha-ras. The levels in 416B cells of the two Ki-ras RNAs, sized 5.2 and 2.0 kilobases, were both elevated approximately 25-fold over levels found in normal mouse cells; there was no corresponding change in 416B cells in the levels of the two Ha-ras RNAs. We partially purified the two Ki-ras mRNAs and separated them by velocity sedimentation in sucrose density gradients. Both the 5.2- and 2.0-kilobase mRNAs could be translated in vitro into p21 ras. These results show that a cellular onc protein can be translated from two distinct cellular mRNA species.

Sign in / Sign up

Export Citation Format

Share Document