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Title: Primary structure of the human fgr proto-oncogene product p55/sup c-fgr/

Abstract

Normal human c-fgr cDNA clones were constructed by using normal peripheral blood mononuclear cell mRNA as a template. Nucleotide sequence analysis of two such clones revealed a 1,587-base-pair-long open reading frame which predicted the primary amino acid sequence of the c-fgr translational product. Homology of this protein with the v-fgr translational product stretched from codons 128 to 516, where 32 differences among 388 codons were observed. Sequence similarity with human c-src, c-yes, and fyn translations products began at amino acid position 76 of the predicted c-fgr protein and extended nearly to its C-terminus. In contrast, the stretch of 75 amino acids at the N-terminus demonstrated a greatly reduced degree of relatedness to these same proteins. To verify the deduced amino acid sequence, antibodies were prepared against peptides representing amino- and carboxy-terminal regions of the predicted c-fgr translational product. Both antibodies specifically recognized a 55-kilodalton protein expressed in COS-1 cells transfected with a c-fgr cDNA expression plasmid. Moreover, the same protein was immunoprecipitated from an Epstein-Barr virus-infected Burkitt's lymphoma cell line which expressed c-fgr mRNA but not in its uninfected fgr mRNA-negative counterpart. These findings identified the 55-kilodalton protein as the product of the human fgr proto-oncogene.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Lab. of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD (US)
OSTI Identifier:
7077510
Resource Type:
Journal Article
Resource Relation:
Journal Name: Mol. Cell. Biol.; (United States); Journal Volume: 8:1
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; NUCLEOPROTEINS; AMINO ACID SEQUENCE; DNA SEQUENCING; ONCOGENES; STRUCTURE-ACTIVITY RELATIONSHIPS; CELL CULTURES; DNA-CLONING; GENETIC MAPPING; IMMUNOASSAY; LYMPHOMAS; MAN; MESSENGER-RNA; MOLECULAR BIOLOGY; MONOCYTES; PHENOTYPE; ANIMALS; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CLONING; DISEASES; GENES; IMMUNE SYSTEM DISEASES; LEUKOCYTES; MAMMALS; MAPPING; MATERIALS; MOLECULAR STRUCTURE; NEOPLASMS; NUCLEIC ACIDS; ORGANIC COMPOUNDS; PRIMATES; PROTEINS; RNA; STRUCTURAL CHEMICAL ANALYSIS; VERTEBRATES; 550200* - Biochemistry; 550400 - Genetics

Citation Formats

Katamine, S., Notario, V., Rao, C.D., Miki, T., Cheah, M.S.C., Tronick, S.R., and Robbins, K.C.. Primary structure of the human fgr proto-oncogene product p55/sup c-fgr/. United States: N. p., 1988. Web. doi:10.1128/MCB.8.1.259.
Katamine, S., Notario, V., Rao, C.D., Miki, T., Cheah, M.S.C., Tronick, S.R., & Robbins, K.C.. Primary structure of the human fgr proto-oncogene product p55/sup c-fgr/. United States. doi:10.1128/MCB.8.1.259.
Katamine, S., Notario, V., Rao, C.D., Miki, T., Cheah, M.S.C., Tronick, S.R., and Robbins, K.C.. Fri . "Primary structure of the human fgr proto-oncogene product p55/sup c-fgr/". United States. doi:10.1128/MCB.8.1.259.
@article{osti_7077510,
title = {Primary structure of the human fgr proto-oncogene product p55/sup c-fgr/},
author = {Katamine, S. and Notario, V. and Rao, C.D. and Miki, T. and Cheah, M.S.C. and Tronick, S.R. and Robbins, K.C.},
abstractNote = {Normal human c-fgr cDNA clones were constructed by using normal peripheral blood mononuclear cell mRNA as a template. Nucleotide sequence analysis of two such clones revealed a 1,587-base-pair-long open reading frame which predicted the primary amino acid sequence of the c-fgr translational product. Homology of this protein with the v-fgr translational product stretched from codons 128 to 516, where 32 differences among 388 codons were observed. Sequence similarity with human c-src, c-yes, and fyn translations products began at amino acid position 76 of the predicted c-fgr protein and extended nearly to its C-terminus. In contrast, the stretch of 75 amino acids at the N-terminus demonstrated a greatly reduced degree of relatedness to these same proteins. To verify the deduced amino acid sequence, antibodies were prepared against peptides representing amino- and carboxy-terminal regions of the predicted c-fgr translational product. Both antibodies specifically recognized a 55-kilodalton protein expressed in COS-1 cells transfected with a c-fgr cDNA expression plasmid. Moreover, the same protein was immunoprecipitated from an Epstein-Barr virus-infected Burkitt's lymphoma cell line which expressed c-fgr mRNA but not in its uninfected fgr mRNA-negative counterpart. These findings identified the 55-kilodalton protein as the product of the human fgr proto-oncogene.},
doi = {10.1128/MCB.8.1.259},
journal = {Mol. Cell. Biol.; (United States)},
number = ,
volume = 8:1,
place = {United States},
year = {Fri Jan 01 00:00:00 EST 1988},
month = {Fri Jan 01 00:00:00 EST 1988}
}
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