scholarly journals Nucleotide sequence of the src gene of the Schmidt - Ruppin strain of Rous Sarcoma virus type E

1989 ◽  
Vol 17 (3) ◽  
pp. 1252-1252 ◽  
Author(s):  
Jean Vianney Barnier ◽  
Philippe Dezélée ◽  
Maria Marx ◽  
Georges Calothy
Keyword(s):  
Nucleotide Sequence ◽  
Virus Type ◽  
Rous Sarcoma Virus ◽  
Rous Sarcoma ◽  
Src Gene ◽  
Sarcoma Virus

scholarly journals Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src.

1985 ◽  
Vol 5 (5) ◽  
pp. 1122-1129 ◽  
Author(s):  
S K Anderson ◽  
C P Gibbs ◽  
A Tanaka ◽  
H J Kung ◽  
D J Fujita
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Rous Sarcoma Virus ◽  
Cellular Growth ◽  
Tyrosine Kinase Domain ◽  
Rous Sarcoma ◽  
Src Gene ◽  
Sarcoma Virus ◽  
Carboxy Terminal

The nucleotide sequence of the 3' two-thirds of a highly conserved, molecularly cloned human cellular src gene (c-src) has been determined. This region of the c-src gene encodes the tyrosine kinase domain of the cellular src protein (pp60c-src) and corresponds to exons 6 through 12 of the chicken c-src gene, as well as nucleotides 545 to 1542 of the Rous sarcoma virus src gene (v-src). The human c-src sequence is very strongly conserved with respect to both the chicken c-src and the Rous sarcoma virus v-src genes, with nearly 90% nucleotide homology observed in this region. Amino acid sequence conservation in this region is even greater; 98% of the amino acids are conserved between human and chicken c-src. Furthermore, the exon sizes and the locations of the exon-intron boundaries are identical in the human and chicken c-src genes. However, sequences within the introns have not been conserved, and the introns within the human c-src gene are significantly larger than the corresponding introns within the chicken c-src gene. The strong amino acid conservation between the carboxy-terminal two-thirds of pp60c-src of species as divergent as humans and chickens suggests that this portion of the pp60c-src protein specifies one or more functional domains that are of great importance to some aspect of normal cellular growth or differentiation.

Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src

1985 ◽  
Vol 5 (5) ◽  
pp. 1122-1129
Author(s):  
S K Anderson ◽  
C P Gibbs ◽  
A Tanaka ◽  
H J Kung ◽  
D J Fujita
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Rous Sarcoma Virus ◽  
Cellular Growth ◽  
Tyrosine Kinase Domain ◽  
Rous Sarcoma ◽  
Src Gene ◽  
Sarcoma Virus ◽  
Carboxy Terminal

The nucleotide sequence of the 3' two-thirds of a highly conserved, molecularly cloned human cellular src gene (c-src) has been determined. This region of the c-src gene encodes the tyrosine kinase domain of the cellular src protein (pp60c-src) and corresponds to exons 6 through 12 of the chicken c-src gene, as well as nucleotides 545 to 1542 of the Rous sarcoma virus src gene (v-src). The human c-src sequence is very strongly conserved with respect to both the chicken c-src and the Rous sarcoma virus v-src genes, with nearly 90% nucleotide homology observed in this region. Amino acid sequence conservation in this region is even greater; 98% of the amino acids are conserved between human and chicken c-src. Furthermore, the exon sizes and the locations of the exon-intron boundaries are identical in the human and chicken c-src genes. However, sequences within the introns have not been conserved, and the introns within the human c-src gene are significantly larger than the corresponding introns within the chicken c-src gene. The strong amino acid conservation between the carboxy-terminal two-thirds of pp60c-src of species as divergent as humans and chickens suggests that this portion of the pp60c-src protein specifies one or more functional domains that are of great importance to some aspect of normal cellular growth or differentiation.

Corrections to the nucleotide sequence of the src gene of Rous sarcoma virus

Nature ◽  
1983 ◽  
Vol 301 (5902) ◽  
pp. 736-738 ◽  
Author(s):  
A. PETER CZERNILOFSKY ◽  
ARTHUR D. LEVINSON ◽  
HAROLD E. VARMUS ◽  
J. MICHAEL BISHOP ◽  
EDWARD TISCHER ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Rous Sarcoma Virus ◽  
Rous Sarcoma ◽  
Src Gene ◽  
Sarcoma Virus

Functional domains of the pp60v-src protein as revealed by analysis of temperature-sensitive Rous sarcoma virus mutants

1984 ◽  
Vol 4 (8) ◽  
pp. 1508-1514
Author(s):  
A W Stoker ◽  
P J Enrietto ◽  
J A Wyke
Keyword(s):  
Rous Sarcoma Virus ◽  
Kinase Activity ◽  
Temperature Sensitive ◽  
Tyrosine Kinase Activity ◽  
Rous Sarcoma ◽  
Heat Labile ◽  
Src Gene ◽  
Sarcoma Virus

Four temperature-sensitive (ts) Rous sarcoma virus src gene mutants with lesions in different parts of the gene represent three classes of alteration in pp60src. These classes are composed of mutants with (i) heat-labile protein kinase activities both in vitro and in vivo (tsLA27 and tsLA29), (ii) heat-labile kinases in vivo but not in vitro (tsLA33), and (iii) neither in vivo nor in vitro heat-labile kinases (tsLA32). The latter class indicates the existence of structural or functional pp60src domains that are required for transformation but do not grossly affect tyrosine kinase activity.

scholarly journals Expression of the chicken c-src gene in COS cells

1984 ◽  
Vol 4 (5) ◽  
pp. 846-851
Author(s):  
T M Gilmer
Keyword(s):  
Rous Sarcoma Virus ◽  
Recombinant Plasmid ◽  
Expression System ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Cos Cells ◽  
Rous Sarcoma ◽  
Src Gene ◽  
Cellular Homolog ◽  
Sarcoma Virus

The cellular homolog of the Rous sarcoma virus transforming gene (v-src) was cloned into a plasmid containing the simian virus 40 origin of replication and transcriptional signals. This recombinant plasmid, designated pSVOHCS11 , directs the synthesis of relatively high levels of c-src mRNA and c-src protein ( pp60c -src), when the plasmid is studied 48 to 72 h after calcium phosphate-mediated DNA transfection of COS (monkey) cells. The level of c-src mRNA synthesis is 50-fold higher than the amount of c-src RNA produced in uninfected chicken embryo fibroblasts. Furthermore, the level of pp60c -src expressed in pSVOHCS11 -transfected COS cells is approximately the same as that of pp60v -src in Rous sarcoma virus-transformed cells. Using this recombinant plasmid, we demonstrated that c-src mRNA contains sequences which map 3' to the previously identified c-src-v-src regions of homology. In view of the small amount of c-src mRNA and protein that can be isolated from uninfected cells, this transient expression system offers a convenient source of material for further analyses of the c-src gene product.

scholarly journals Highly specific antibody to Rous sarcoma virus src gene product recognizes a novel population of pp60v-src and pp60c-src molecules.

1985 ◽  
Vol 100 (2) ◽  
pp. 409-417 ◽  
Author(s):  
M D Resh ◽  
R L Erikson
Keyword(s):  
Plasma Membrane ◽  
Specific Antibody ◽  
Rous Sarcoma Virus ◽  
Distinct Pattern ◽  
Cell Periphery ◽  
Equal Distribution ◽  
Rous Sarcoma ◽  
Src Gene ◽  
Sarcoma Virus ◽  
Infected Cells

Antiserum to the Rous sarcoma virus (RSV)-transforming protein, pp60v-src, was produced in rabbits immunized with p60 expressed in Escherichia coli. alpha p60 serum immunoprecipitated quantitatively more pp60v-src than did tumor-bearing rabbit (TBR) sera. When RSV-transformed cell lysates were preadsorbed with TBR serum, the remaining lysate contained additional pp60v-src, which was recognized only by reimmunoprecipitation with alpha p60 serum and not by TBR serum. In subcellular fractions of RSV-infected chicken embryo fibroblasts (RSV-CEFs) and field vole cells probed with TBR serum, the majority of the pp60v-src was associated with the plasma membrane-enriched P100 fraction. However, alpha p60 serum revealed equal distribution of pp60v-src and its kinase activity between the P1 (nuclear) and P100 fractions. The same results were obtained for pp60c-src in uninfected CEFs. On discontinuous sucrose gradients nearly 50% of the P1-pp60v-src sedimented with nuclei, in fractions where no plasma membrane was detected. Indirect immunofluorescence microscopy of RSV-CEFs with alpha p60 serum revealed a distinct pattern of perinuclear fluorescence, in addition to staining at the cell periphery. Thus the use of a highly specific antibody reveals that enzymatically active pp60v-src and pp60c-src molecules are present in other intracellular structures, probably juxtareticular nuclear membranes, in addition to the plasma membrane in normal, uninfected, and wild-type RSV-infected cells.

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