Journal
MOLECULAR CELL
Volume 65, Issue 5, Pages 861-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2017.01.026
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Funding
- Max Planck Institute of Biochemistry
- Max Planck Society
- University of Lausanne
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SMC proteins support vital cellular processes in all domains of life by organizing chromosomal DNA. They are composed of ATPase head and hinge dimerization domains and a connecting coiled-coil arm. Binding to a kleisin subunit creates a closed tripartite ring, whose similar to 47-nm-long SMC arms act as barrier for DNA entrapment. Here, we uncover another, more active function of the bacterial Smc arm. Using high-throughput genetic engineering, we resized the arm in the range of 6-60 nm and found that it was functional only in specific length regimes following a periodic pattern. Natural SMC sequences reflect these length constraints. Mutants with improper arm length or peptide insertions in the arm efficiently target chromosomal loading sites and hydrolyze ATP but fail to use ATP hydrolysis for relocation onto flanking DNA. We propose that SMC arms implement force transmission upon nucleotide hydrolysis to mediate DNA capture or loop extrusion.
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