1. ABSTRACT Myosins are proteins that convert chemical energy stored in ATP into mechanical force that is applied on an actin filament. Nuclear myosin 1 (NM1) was the first myosin detected in the cell nucleus. Together with nuclear actin they were shown to play important roles in DNA transcription and chromatin remodeling. However, the molecular details of the NM1 functions are largely unknown. To expand our knowledge about this molecular motor we studied tissue expression, mechanism of nuclear localization and molecular interactions of this myosin motor. In the first part we examined the expression pattern of NM1 in various mouse tissues. We demonstrated that NM1 is present in cell nuclei of all mouse tissues examined except for cells in terminal stages of spermatogenesis. Quantitative PCR and western blots demonstrated that the expression of NM1 in tissues varies, with the highest levels in the lungs. NM1 is a nuclear isoform of earlier identified myosin 1c (Myo1c), which was described initially as a cytosolic, and plasma membrane associated protein. The only known difference between these two proteins was the presence of additional 16 amino acids at the N-terminus of NM1. Next we focused on the influence of NM1 domains, including the N-terminus, on the subcellular localization of this protein. We found...
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:311784 |
| Date | January 2012 |
| Creators | Dzijak, Rastislav |
| Contributors | Hozák, Pavel, Hašek, Jiří, Kaňka, Jiří |
| Source Sets | Czech ETDs |
| Language | English |
| Detected Language | English |
| Type | info:eu-repo/semantics/doctoralThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
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