Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability
[摘要] Ca2+ pump dimerization was studied by using a combined approach of thermal denaturation and fluorescence resonance energy transfer. The measurement of calcium pump ability to dimerize after the unfolding of individual functional domains of the enzyme demonstrated the existence of two different regions involved in the self-association process. One of these regions is highly susceptible to thermal unfolding and was identified as the calmodulin (CaM)-binding domain. The other region whose thermal stability is higher than those of the catalytic and CaM-binding domains could be related with the previously found C28W-binding regions.
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[效力级别] [学科分类] 生物化学/生物物理
[关键词] Calcium pump;Oligomerization;Thermal stability;Plasma membrane calcium pump;Calmodulin;Membrane protein;C28W;synthetic peptide corresponding to the sequence 1086–1113 of the hPMCA4b;CaM;calmodulin;EITC;eosin-5′-isothiocyanate;FITC;fluorescein-5′-isothiocyanate;FRET;fluorescence resonance energy transfer;hPMCA4b;isoform 4b of the human plasma membrane calcium pump;MOPS;3-(N-morpholino)-propanesulfonic acid;PMCA;human plasma membrane calcium pump;PMSF;phenylmethyl-sulfonyl fluoride [时效性]
