Prothymosin α fragmentation in apoptosis
| Autor: | Vadim I. Agol, George A. Belov, Markus Kalkum, Nina V. Chichkova, Andrey B. Vartapetian, Alexandra G. Evstafieva, Alexey A. Bogdanov |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Nuclear Localization Signals
Biophysics Peptide Apoptosis DNA Fragmentation Prothymosin Alpha Cleavage (embryo) Transfection Biochemistry Nuclear localization signal Structural Biology Genetics Humans Nuclear protein Protein Precursors Molecular Biology Caspase chemistry.chemical_classification Caspase 7 Binding Sites biology Chemistry Caspase 3 Prothymosin α Cell Biology Molecular biology In vitro Cell biology Thymosin Caspases biology.protein Nuclear localization sequence hormones hormone substitutes and hormone antagonists HeLa Cells |
| Zdroj: | FEBS Letters. (2-3):150-154 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(00)01139-X |
| Popis: | We observed fragmentation of an essential proliferation-related human nuclear protein prothymosin alpha in the course of apoptosis induced by various stimuli. Prothymosin alpha cleavage occurred at the DDVD(99) motif. In vitro, prothymosin alpha could be cleaved at D(99) by caspase-3 and -7. Caspase hydrolysis disrupted the nuclear localization signal of prothymosin alpha and abrogated the ability of the truncated protein to accumulate inside the nucleus. Prothymosin alpha fragmentation may therefore be proposed to disable intranuclear proliferation-related function of prothymosin alpha in two ways: by cleaving off a short peptide containing important determinants, and by preventing active nuclear uptake of the truncated protein. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|