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XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

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Lectures<br />

LIPID HELICES formaTION IN BaCILLUS SUBTILIS CELL MEMBraNE<br />

Imrich Barák, Katarína Muchová, Nada Pavlendová and Ján Jamroškovič<br />

Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská cesta 21,<br />

845 51 Bratislava, Slovakia<br />

The domains of different lipid composition are present in eukaryotic and prokaryotic cell<br />

membranes. Using membrane binding fluorescent dyes, we demonstrate previously, the<br />

presence of lipid spirals extending along the long-axis of cells of the rod-shaped bacterium<br />

B. subtilis. These data indicate a higher level of membrane lipid organization than<br />

previously observed. Little is known however of the origin of these helical structures.<br />

Principally, there are at least three main specifically localized molecular structures in<br />

the membrane or close proximity to it what can help to form or influence the formation<br />

of lipid helixes. In our work we have focused on analyzing these lipid structures in correlation<br />

with other above mentioned helical structures in the cell membrane or its close<br />

proximity. We were analyzing lipid domains by using lipid specific dyes in protoplasted<br />

cells, in Mbl, MreB and MreBH mutant strains. We have used FRAP and FRET experiments<br />

to determine dynamics of lipid domains and co-localization of lipid dyes with GFP fused<br />

proteins, respectively.<br />

We have also studied the role of lipid helices in cell division by directing the Min system<br />

to the helices from pole to pole. We inspected cell division when E. coli Min-system was<br />

introduced into B. subtilis cells. We show that MinD Ec<br />

can partially substitute function of<br />

its B. subtilis protein counterpart. Additionally, we observed dynamic behavior of MinD Ec<br />

and MinE in B. subtilis when expressed together. All these findings indicate that these<br />

two Min systems resemble each other more than was thought previously<br />

42 <strong>XXII</strong>. Biochemistry Congress, Martin

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