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A 53-kilodalton protein common to chemically and virally transformed cells shows extensive sequence similarities between species.
- Source :
- Proceedings of the National Academy of Sciences of the United States of America; January 1982, Vol. 79 Issue: 2 p287-291, 5p
- Publication Year :
- 1982
-
Abstract
- A heat-stable DNA-binding protein with subunits of about 53 kilodaltons (kDal) was purified from two virally transformed human cell lines (Epstein-Barr virus-positive Raji and Namalwa) and two mouse tumor cell lines (methylcholanthrene-induced Meth A sarcoma and TA3 mammary carcinoma). All four 53kDal proteins showed closely related total amino acid compositions, similar peptide maps, and identical NH2-terminal amino acid sequences for 20 residues. These 53-kDal proteins are therefore evolutionarily highly conserved, independent of whether they originate from virally or chemically transformed cells. The NH2-terminal sequence and the protein chain as a whole are not hydrophobic; however, some unexpected residue distributions were observed. Comparisons with other proteins reveal no clear sequence similarity with known tumor antigen structures, homologous immunoglobulins, or some other proteins of known sequence. Epstein-Barr virus-determined nuclear antigen also appears to have a different NH2-terminal sequence. Thus, the results show that the 53-kDal proteins represent a unique protein type with little species variation; this finding suggests that these proteins must perform an important common function in different transformation systems.
Details
- Language :
- English
- ISSN :
- 00278424 and 10916490
- Volume :
- 79
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Periodical
- Accession number :
- ejs60438940
- Full Text :
- https://doi.org/10.1073/pnas.79.2.287