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Your search keyword '"Diebold-Durand ML"' showing total 3 results
Start Over Author "Diebold-Durand ML" Topic chromosomes, bacterial
3 results on '"Diebold-Durand ML"'

1. Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization.

Author

Diebold-Durand ML, Lee H, Ruiz Avila LB, Noh H, Shin HC, Im H, Bock FP, Bürmann F, Durand A, Basfeld A, Ham S, Basquin J, Oh BH, and Gruber S

Subjects
Adenosine Triphosphate metabolism, Bacillus subtilis genetics, Bacterial Proteins chemistry, Bacterial Proteins genetics, Binding Sites, Cell Cycle Proteins chemistry, Cell Cycle Proteins genetics, Crystallography, X-Ray, Cysteine, High-Throughput Screening Assays, Models, Molecular, Mutation, Nucleic Acid Conformation, Protein Conformation, Protein Multimerization, Protein Stability, Structure-Activity Relationship, Bacillus subtilis metabolism, Bacterial Proteins metabolism, Cell Cycle Proteins metabolism, Chromosome Segregation, Chromosomes, Bacterial
Abstract

Multi-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double helices. SMC subunits comprise an ABC ATPase "head" and a "hinge" dimerization domain connected by a 49 nm coiled-coil "arm." The heads undergo ATP-dependent engagement and disengagement to drive SMC action on the chromosome. Here, we elucidate the architecture of prokaryotic Smc dimers by high-throughput cysteine cross-linking and crystallography. Co-alignment of the Smc arms tightly closes the interarm space and misaligns the Smc head domains at the end of the rod by close apposition of their ABC signature motifs. Sandwiching of ATP molecules between Smc heads requires them to substantially tilt and translate relative to each other, thereby opening up the Smc arms. We show that this mechanochemical gating reaction regulates chromosome targeting and propose a mechanism for DNA translocation based on the merging of DNA loops upon closure of Smc arms., (Copyright © 2017 The Authors. Published by Elsevier Inc. All rights reserved.)

Published
2017
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2. 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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3. 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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