Charakterizace membránového proteinu DREPP
Characterization of membrane protein DREPP
diplomová práce (OBHÁJENO)

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Trvalý odkaz
http://hdl.handle.net/20.500.11956/31373Identifikátory
SIS: 63523
Kolekce
- Kvalifikační práce [20352]
Autor
Vedoucí práce
Konzultant práce
Fischer, Lukáš
Oponent práce
Cvrčková, Fatima
Fakulta / součást
Přírodovědecká fakulta
Obor
Anatomie a fyziologie rostlin
Katedra / ústav / klinika
Katedra experimentální biologie rostlin
Datum obhajoby
9. 9. 2010
Nakladatel
Univerzita Karlova, Přírodovědecká fakultaJazyk
Čeština
Známka
Výborně
Klíčová slova (česky)
huseníček, tabák, mikrotubuly, plasmatická membrána, cytoskeletKlíčová slova (anglicky)
Arabidopsis thaliana, Nicotiana tabacum, DREPP, developmentally regulated plasma membrane polypeptide, PCaP1, PCaP2, plasma membrane-asociated cation-binding protein, MAP18, microtubule-asociated protein, GFP fusion, biolistic, plasma membrane, microtubulProteins of DREPP family (20-25 kDa, syn. PCaP1 in Arabidopsis thaliana) first appeared in ferns and we have shown that several independent duplications of DREPP protein occurred during evolution of large families (Poaceae, Brassicaceae, Solanaceae and Asteraceae) and in group Coniferophyta. Secondary losses of one paralogue occurred in subfamilies Pooideae and Solanoideae.We have also detected two large-scale modification of DREEP protein in Asparagales and Brassicaceae (this divergent paralogue was previously described as MAP18 protein). We have examined colinearity of chromosome fragments in vicinity both PCaP1 and MAP18 paralogues in Arabidopsis thaliana and we hypothesize that MAP18 gene arose during genome duplication on the origin of Brassicaceae family. DREPP protein was previously identified in detergent-resistant membrane microdomain fraction and a myristyl anchor was shown to be necessary for their membrane localization. Membrane association was shown to be modified by the interaction of unique N-terminal domain with PtdInsPs, which was inhibited by binding of Ca-calmodulin (Nagasaki et al., 2008). The mutation of Gly2 by Ala in the myristilation site, or C-terminal GFP-fusion (GFP-DREPP), affect membrane association in Arabidopsis thaliana (Nagasaki et al., 2008). Several DREPP paralogues in...