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Tuned SMC Arms Drive Chromosomal Loading of Prokaryotic Condensin.
- Source :
-
Molecular cell [Mol Cell] 2017 Mar 02; Vol. 65 (5), pp. 861-872.e9. Date of Electronic Publication: 2017 Feb 23. - Publication Year :
- 2017
-
Abstract
- 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 ∼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.<br /> (Copyright © 2017 The Author(s). Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Adenosine Triphosphatases chemistry
Adenosine Triphosphatases genetics
Adenosine Triphosphate metabolism
Bacillus subtilis genetics
Bacterial Proteins chemistry
Bacterial Proteins genetics
Binding Sites
Cell Cycle Proteins chemistry
Cell Cycle Proteins genetics
Chromosomes, Bacterial chemistry
Chromosomes, Bacterial genetics
DNA, Bacterial chemistry
DNA, Bacterial genetics
DNA-Binding Proteins chemistry
DNA-Binding Proteins genetics
Genetic Engineering methods
High-Throughput Screening Assays
Hydrolysis
Multiprotein Complexes chemistry
Multiprotein Complexes genetics
Mutation
Nucleic Acid Conformation
Protein Binding
Protein Conformation, alpha-Helical
Structure-Activity Relationship
Adenosine Triphosphatases metabolism
Bacillus subtilis enzymology
Bacterial Proteins metabolism
Cell Cycle Proteins metabolism
Chromosomes, Bacterial enzymology
DNA, Bacterial metabolism
DNA-Binding Proteins metabolism
Multiprotein Complexes metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1097-4164
- Volume :
- 65
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 28238653
- Full Text :
- https://doi.org/10.1016/j.molcel.2017.01.026