Identification of nuclear-import and cell-cycle regulatory proteins that bind to prothymosin α
| Autor: | Cristina Díaz-Jullien, Manuel Freire, Javier Freire, Guillermo Covelo, C.S. Sarandeses |
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| Rok vydání: | 2001 |
| Předmět: | |
| Zdroj: | Biochemistry and Cell Biology. 79:123-131 |
| ISSN: | 1208-6002 0829-8211 |
| Popis: | Prothymosin α (ProTα) is a nuclear protein that is widely distributed in mammalian tissues, and is thought to play a role in cell proliferation. In an attempt to shed light on this role, affinity chromatography on ProTα-Sepharose columns was used to identify proteins in subcellular extracts of transformed human lymphocytes (NC37 cells) that interact with ProTα in vitro, and thus may interact with ProTα in vivo. Immunoblotting techniques were used to screen the ProTα-binding fractions for histones and other proteins involved in nuclear transport and cell-cycle control. The most abundant ProTα-binding proteins were histones H2A, H2B, H3, and H4. Of the nuclear-transport proteins, karyopherin β1, Rch-1, Ran, and RCC1 were detected at high concentrations; NTF2, nucleoporin p62, and Hsp70 were detected at low concentrations; while tranportin, CAS, and Ran BP1 were not detected. Of the cell-cycle control proteins, PCNA, Cdk2, and cyclin A were detected at high concentrations; cdc2, Cdk4, and cyclin B were detected at very low concentrations; while cyclin D1, cyclin D3, Cip1, and Kip1 were not detected. These results suggest (i) that ProTα is transported into the nucleus by the karyopherin β1- Rch-1 complex, and (ii) that ProTα may interact in the nucleus with proteins involved in DNA metabolism and cell-cycle control.Key words: prothymosin α, histone-binding proteins, nuclear transport proteins, cell-cycle proteins, chromatin remodeling. |
| Databáze: | OpenAIRE |
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