Architecture of prokaryotic condensin

<p style="text-align: justify;">Model of chromosomal DNA entrapped by prokaryotic condensin rings.</p>

Model of chromosomal DNA entrapped by prokaryotic condensin rings.

Research

What holds a chromosome together at its core?

Chromosomes contain up to a few billion nucleobases that are spliced into extraordinarily long, interwound strands of DNA. Before a cell divides, these tangly molecules must be confined to (much) less than half of the volume of the cell and fully separated from their identical copies. SMC protein complexes form highly elongated, ATPases with a ring topology that play key roles in the shaping of chromosomes in all branches of life. Condensin is pivotal for the striking reorganization of chromosomes during mitosis and ensures timely separation of sister chromatids during anaphase. Similarly, in bacteria Smc–ScpAB promotes efficient segregation of chromosomes in rapidly dividing cells, presumably by compacting and resolving sister DNA molecules.

Our goal is to uncover basic mechanisms by which molecular machines help to disentangle and compact giant chromosomal DNA molecules to enable their proper segregation. We are focussing on the molecular architecture, biochemical activity and cellular function of SMC protein complexes using for most of our studies bacteria and yeast as tractable model systems.

For our research we are utilizing live cell imaging, chemical biology, biophysical analysis of protein-DNA interactions, structural biology and chromosome conformation capture, which represent a powerful combination of methods to investigate the biology of chromosome dynamics.

 

 
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