Amino-terminal domain of the v-fms oncogene product includes a functional signal peptide that directs synthesis of a transforming glycoprotein in the absence of feline leukemia virus gag sequences
Journal Article
·
· J. Virol.; (United States)
OSTI ID:6142842
The nucleotide sequence of a 5' segment of the human genomic c-fms proto-oncogene suggested that recombination between feline leukemia virus and feline c-fms sequences might have occurred in a region encoding the 5' untranslated portion of c-fms mRNA. The polyprotein precursor gP180/sup gag-fms/ encoded by the McDonough strain of feline sarcoma virus was therefore predicted to contain 34 v-fms-coded amino acids derived from sequences of the c-fms gene that are not ordinarily translated from the proto-oncogene mRNA. The (gP180/sup gag-fms/) polyprotein was cotranslationally cleaved near the gag-fms junction to remove its gag gene-coded portion. Determination of the amino-terminal sequence of the resulting v-fms-coded glycoprotein, gp120/sup v-fms/, showed that the site of proteolysis corresponded to a predicted signal peptidase cleavage site within the c-fms gene product. Together, these analyses suggested that the linked gag sequences may not be necessary for expression of a biologically active v-fms gene product. The gag-fms sequences of feline sarcoma virus strain McDonough and the v-fms sequences alone were inserted into a murine retroviral vector containing a neomycin resistance gene. The authors conclude that a cryptic hydrophobic signal peptide sequence in v-fms was unmasked by gag deletion, thereby allowing the correct orientation and transport of the v-fms was unmasked by gag deletion, thereby allowing the correct orientation and transport of the v-fms gene product within membranous organelles. It seems likely that the proteolytic cleavage of gP180/gag-fms/ is mediated by signal peptidase and that the amino termini of gp140/sup v-fms/ and the c-fms gene product are identical.
- Research Organization:
- St. Jude Children's Research Hospital, Memphis, TN (USA)
- OSTI ID:
- 6142842
- Journal Information:
- J. Virol.; (United States), Journal Name: J. Virol.; (United States) Vol. 59:2; ISSN JOVIA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOSYNTHESIS
CARBOHYDRATES
CARBOXYLIC ACIDS
CATS
DAYS LIVING RADIOISOTOPES
DNA SEQUENCING
DRUGS
ELECTROPHORESIS
EVEN-ODD NUCLEI
GENE REGULATION
GENES
GLUCOPROTEINS
GLYCOPROTEINS
ISOTOPES
LEUKEMIA VIRUSES
LIGHT NUCLEI
LIPOTROPIC FACTORS
MAMMALS
METHIONINE
MICROORGANISMS
MOLECULAR STRUCTURE
MUTATIONS
NUCLEI
ONCOGENES
ONCOGENIC VIRUSES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PARASITES
PEPTIDES
PROTEINS
RADIOISOTOPES
SACCHARIDES
STRUCTURAL CHEMICAL ANALYSIS
SULFUR 35
SULFUR ISOTOPES
SYNTHESIS
VERTEBRATES
VIRUSES
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOSYNTHESIS
CARBOHYDRATES
CARBOXYLIC ACIDS
CATS
DAYS LIVING RADIOISOTOPES
DNA SEQUENCING
DRUGS
ELECTROPHORESIS
EVEN-ODD NUCLEI
GENE REGULATION
GENES
GLUCOPROTEINS
GLYCOPROTEINS
ISOTOPES
LEUKEMIA VIRUSES
LIGHT NUCLEI
LIPOTROPIC FACTORS
MAMMALS
METHIONINE
MICROORGANISMS
MOLECULAR STRUCTURE
MUTATIONS
NUCLEI
ONCOGENES
ONCOGENIC VIRUSES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PARASITES
PEPTIDES
PROTEINS
RADIOISOTOPES
SACCHARIDES
STRUCTURAL CHEMICAL ANALYSIS
SULFUR 35
SULFUR ISOTOPES
SYNTHESIS
VERTEBRATES
VIRUSES