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2 results on '"Diebold-Durand ML"'

1. Tuned SMC Arms Drive Chromosomal Loading of Prokaryotic Condensin.

Author

Bürmann F, Basfeld A, Vazquez Nunez R, Diebold-Durand ML, Wilhelm L, and Gruber S

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
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., (Copyright © 2017 The Author(s). Published by Elsevier Inc. All rights reserved.)

Published
2017
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2. Control of Smc Coiled Coil Architecture by the ATPase Heads Facilitates Targeting to Chromosomal ParB/parS and Release onto Flanking DNA.

Author

Minnen A, Bürmann F, Wilhelm L, Anchimiuk A, Diebold-Durand ML, and Gruber S

Subjects
Adenosine Triphosphate metabolism, Amino Acid Sequence, Bacillus subtilis genetics, Bacterial Proteins genetics, Cell Cycle Proteins genetics, Cell Division, Chromosome Segregation, Chromosomes, Bacterial ultrastructure, DNA Primase genetics, DNA, Bacterial genetics, Hydrolysis, Isoenzymes genetics, Isoenzymes metabolism, Models, Molecular, Molecular Sequence Data, Protein Domains, Protein Multimerization, Protein Structure, Secondary, Protein Transport, Sequence Alignment, Bacillus subtilis metabolism, Bacterial Proteins metabolism, Cell Cycle Proteins metabolism, Chromosomes, Bacterial chemistry, DNA Primase metabolism, DNA, Bacterial metabolism
Abstract

Smc/ScpAB promotes chromosome segregation in prokaryotes, presumably by compacting and resolving nascent sister chromosomes. The underlying mechanisms, however, are poorly understood. Here, we investigate the role of the Smc ATPase activity in the recruitment of Smc/ScpAB to the Bacillus subtilis chromosome. We demonstrate that targeting of Smc/ScpAB to ParB/parS loading sites is strictly dependent on engagement of Smc head domains and relies on an open organization of the Smc coiled coils. We find that dimerization of the Smc hinge domain stabilizes closed Smc rods and hinders head engagement as well as chromosomal targeting. Conversely, the ScpAB sub-complex promotes head engagement and Smc rod opening and thereby facilitates recruitment of Smc to parS sites. Upon ATP hydrolysis, Smc/ScpAB is released from loading sites and relocates within the chromosome-presumably through translocation along DNA double helices. Our findings define an intermediate state in the process of chromosome organization by Smc., (Copyright © 2016 The Authors. Published by Elsevier Inc. All rights reserved.)

Published
2016
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