TY  - JOUR
A1  - Hundertmark, Michaela
A1  - Dimova, Rumiana
A1  - Lengefeld, Jan
A1  - Seckler, Robert
A1  - Hincha, Dirk K.
T1  - The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding.
N2  - Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. Late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into ;-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport. Research Highlights
Y1  - 2011
SN  - 0006-3002
ER  - 
TY  - THES
A1  - Dimova, Rumiana
T1  - Probing the membrane nanoregime with optical microscopy
Y1  - 2011
CY  - Potsdam
ER  - 
TY  - JOUR
A1  - Hundertmark, Michaela
A1  - Dimova, Rumiana
A1  - Lengefeld, Jan
A1  - Seckler, Robert
A1  - Hincha, Dirk K.
T1  - The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding
JF  - Biochimica et biophysica acta : Biomembranes
N2  - Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into beta-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport.
KW  - Intrinsically disordered protein
KW  - Late embryogenesis abundant protein
KW  - Membrane stability
KW  - Protein-membrane interaction
KW  - Protein folding
Y1  - 2011
U6  - https://doi.org/10.1016/j.bbamem.2010.09.010
SN  - 0005-2736
VL  - 1808
IS  - 1
SP  - 446
EP  - 453
PB  - Elsevier
CY  - Amsterdam
ER  -