Studium struktury a dynamiky proteinů a proteinových komplexů.
5 Abstract Inside the cellular milieu, proteins are reaching their native conformation with the assistance of molecular chaperones. These high mass dynamic complexes perform other functions that are contributing to the stability of the cellular proteome. Transport of proteins into the target compart...
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| Format: | Doctoral Thesis |
| Language: | Czech |
| Published: |
2020
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| Online Access: | http://www.nusl.cz/ntk/nusl-437204 |
| Summary: | 5 Abstract Inside the cellular milieu, proteins are reaching their native conformation with the assistance of molecular chaperones. These high mass dynamic complexes perform other functions that are contributing to the stability of the cellular proteome. Transport of proteins into the target compartment or defence against oxidative stress rank among these as well. Dynamic structural changes of chaperones Hsp70 and NQO1 and co-chaperone Tomm34 that are participating in above mentioned processes and their interactions with ligands are characterized here by the combination of structural mass spectrometry, biophysical and molecular biology techniques. In this thesis the ATP-dependent dimerization of human inducible isoform Hsp70 (HSPA1A) and the characterization of its evolutionarily conserved dimerization interface were described. Further, highly conserved amino acid residues crucial for allosteric movements were identified. These residues create a network of contacts stabilizing both extreme conformations of HSPA1A (low and high-affinity) during the ATPase cycle. One of the co-chaperones that can affect Hsp70 ATPase cycle is TPR co-chaperone Tomm34. This co-chaperone is participating on the transport of the nuclear encoded mitochondrial precursors into the mitochondria. Here we described regulation of this... |
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