ArticleThe Journal of cell biology1998
The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
151 citing papers in PubMed, 373 citations in OpenAlex.
- Condensin complexes: from chromatin organization to disease.Nucleus (Austin, Tex.) · 2026Review
- Structural basis of condensin II activation.Research square · 2026Article
- SMC complex unidirectionally translocates DNA by coupling segment capture with an asymmetric kleisin path.eLife · 2026Article
- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- Spatio-temporal organization of theEcoSal Plus · 2024Review
- DNA sliding and loop formation byBiochemistry and biophysics reports · 2022Article
- Mediator recruits the cohesin loader Scc2 to RNA Pol II-transcribed genes and promotes sister chromatid cohesion.Current biology : CB · 2022Article
- Ubiquity and Origins of Structural Maintenance of Chromosomes (SMC) Proteins in Eukaryotes.Genome biology and evolution · 2021Article
- The Cohesin Complex and Its Interplay with Non-Coding RNAs.Non-coding RNA · 2021Review
- Delineating the Role ofPathogens (Basel, Switzerland) · 2021Article
- Mitotic chromosomes.Seminars in cell & developmental biology · 2021Review
- Structure Basis for Shaping the Nse4 Protein by the Nse1 and Nse3 Dimer within the Smc5/6 Complex.Journal of molecular biology · 2021Article
- Unique Properties of the Alpha-Helical DNA-Binding Protein KfrA Encoded by the IncU Incompatibility Group Plasmid RA3 and Its Host-Dependent Role in Plasmid Maintenance.Applied and environmental microbiology · 2021Article
- Phylogenetic analysis of the ATP-binding cassette proteins suggests a new ABC protein subfamily J in Aedes aegypti (Diptera: Culicidae).BMC genomics · 2020Article
- Modes of action of the archaeal Mre11/Rad50 DNA-repair complex revealed by fast-scan atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nucleoid-mediated positioning and transport in bacteria.Current genetics · 2020Review
- Chromosome organization in bacteria: mechanistic insights into genome structure and function.Nature reviews. Genetics · 2020Review
- Evolutionary repair: Changes in multiple functional modules allow meiotic cohesin to support mitosis.PLoS biology · 2020Article
- Architecture of the Escherichia coli nucleoid.PLoS genetics · 2019Article
- Transient DNA Occupancy of the SMC Interarm Space in Prokaryotic Condensin.Molecular cell · 2019Article
91 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Structural maintenance of chromosomes (SMC) proteins function in chromosome condensation and several other aspects of DNA processing. They are large proteins characterized by an NH2-terminal nucleotide triphosphate (NTP)-binding domain, two long segments of coiled coil separated by a hinge, and a COOH-terminal domain. Here, we have visualized by EM the SMC protein from Bacillus subtilis (BsSMC) and MukB from Escherichia coli, which we argue is a divergent SMC protein. Both BsSMC and MukB show two thin rods with globular domains at the ends emerging from the hinge. The hinge appears to be quite flexible: the arms can open up to 180 degrees, separating the terminal domains by 100 nm, or close to near 0 degrees, bringing the terminal globular domains together. A surprising observation is that the approximately 300-amino acid-long coiled coils are in an antiparallel arrangement. Known coiled coils are almost all parallel, and the longest antiparallel coiled coils known previously are 35-45 amino acids long. This antiparallel arrangement produces a symmetrical molecule with both an NH2- and a COOH-terminal domain at each end. The SMC molecule therefore has two complete and identical functional domains at the ends of the long arms. The bifunctional symmetry and a possible scissoring action at the hinge should provide unique biomechanical properties to the SMC proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.