DNA sliding and loop formation by E. coli SMC complex: MukBEF

Zhou, Maosheng

doi:10.1016/j.bbrep.2022.101297

Cited by 3 publications

(7 citation statements)

References 68 publications

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“…Interestingly, the ability to compact genomic DNA independently of ATP binding and hydrolysis was recently demonstrated for the SMC protein of B. subtilis under in vivo conditions [31], ScpAB modulate this compactization. A similar property was shown for MukB protein -under in vitro conditions this protein compacted DNA in the absence of ATP [12]. Given the relatively low ATP hydrolysis rate by the U. parvum SMC protein, it is important to explore the connection between its ATPase activity and its ability to compact DNA in the future.…”

Section: The Interaction Of U Parvum Smc With Dna Is Enhanced By the ...supporting

confidence: 55%

“…Moreover, SMC-ScpABmediated action results in the formation of a crescent-shaped nucleoid, while the MukBEF complex yields a ring-shaped nucleoid. Notably, while the ability of bacterial SMC complexes to extrude loops under in vitro conditions remains unproven, in vivo findings [13] and some single-molecule experiments conducted in vitro [14,15] support the presence of such capability. SMC complexes likely play indispensable roles in DNA segregation in certain bacterial contexts.…”

Section: Introductionmentioning

confidence: 99%

“…SMC complexes likely play indispensable roles in DNA segregation in certain bacterial contexts. For instance, the MukBEF complex of E. coli is essential during periods of rapid growth [15]. Furthermore, their significance is underscored by their presence in the reduced genomes of Mollicutes; genes encoding proteins of the SMC-ScpAB complex persisted even after directed deletion of approximately half of the genes in a synthetic "minimal bacterium" [16].…”

Section: Introductionmentioning

confidence: 99%

“…Another difference is that the action of SMC-ScpAB leads to the formation of a crescent-shaped nucleoid, whereas in bacteria with the MukBEF complex, a ring nucleoid is formed. Interestingly, the ability to extrude loops under in vitro conditions has not yet been proven for bacterial SMC complexes, although the results obtained in vivo [13], and some results of single-molecule experiments under in vitro conditions [14,15] indicate the presence of such an ability. SMC complexes are probably vital for DNA segregation in at least some bacteria under certain conditions.…”

Section: Introductionmentioning

confidence: 99%

“…SMC complexes are probably vital for DNA segregation in at least some bacteria under certain conditions. For example, the MukBEF complex of E. coli is vital under conditions of rapid growth [15]. Also, the high importance of SMC complexes is indicated by the fact that they are present in reduced Mollicutes genomes; even in the synthetic "minimal bacterium," genes encoding proteins of the SMC-ScpAB complex were conserved after directed deletion of approximately half of the genes [16].…”

Section: Introductionmentioning

confidence: 99%

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Properties of theUreaplasma parvumSMC protein related to its interaction with DNA

Rumyantseva,

Shutov,

Belenkaia

et al. 2024

Preprint

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SMC (Structural Maintenance of Chromosomes) ATPase proteins are a component of complexes of the same name that participate in the spatial organization of DNA in all living organisms - in bacteria, archaea and eukaryotes. In bacteria, SMC complexes perform several functions, among which the function related to DNA condensation and segregation is the most studied. SMC complexes in bacteria are thought to extrude loops and thus compact DNA, as well as promote the separation of daughter nucleoids. In this work, we determined some properties of the SMC ATPase of Ureaplasma parvum, a member of the Mollicutes class with a reduced genome. The results indicate that the properties of this protein differ from those of the well-studied ortholog from Bacillus subtilis, in particular, U. parvum SMC binds to double-stranded DNA rather than single-stranded DNA. This protein has also been shown to compact DNA under in vitro conditions. The ATPase activity of U. parvum SMC was estimated and shown to be induced by DNA binding to SMC. The results of current paper indicate that U. parvum SMC cross-links DNA even in the absence of ATP.

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Section: The Interaction Of U Parvum Smc With Dna Is Enhanced By the ...supporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Properties of theUreaplasma parvumSMC protein related to its interaction with DNA

Rumyantseva,

Shutov,

Belenkaia

et al. 2024

Preprint

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Spatio-temporal organization of the E. coli chromosome from base to cellular length scales

Royzenblat,

Freddolino

2024

EcoSal Plus

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Escherichia coli has been a vital model organism for studying chromosomal structure, thanks, in part, to its small and circular genome (4.6 million base pairs) and well-characterized biochemical pathways. Over the last several decades, we have made considerable progress in understanding the intricacies of the structure and subsequent function of the E. coli nucleoid. At the smallest scale, DNA, with no physical constraints, takes on a shape reminiscent of a randomly twisted cable, forming mostly random coils but partly affected by its stiffness. This ball-of-spaghetti-like shape forms a structure several times too large to fit into the cell. Once the physiological constraints of the cell are added, the DNA takes on overtwisted (negatively supercoiled) structures, which are shaped by an intricate interplay of many proteins carrying out essential biological processes. At shorter length scales (up to about 1 kb), nucleoid-associated proteins organize and condense the chromosome by inducing loops, bends, and forming bridges. Zooming out further and including cellular processes, topological domains are formed, which are flanked by supercoiling barriers. At the megabase-scale both large, highly self-interacting regions (macrodomains) and strong contacts between distant but co-regulated genes have been observed. At the largest scale, the nucleoid forms a helical ellipsoid. In this review, we will explore the history and recent advances that pave the way for a better understanding of E. coli chromosome organization and structure, discussing the cellular processes that drive changes in DNA shape, and what contributes to compaction and formation of dynamic structures, and in turn how bacterial chromatin affects key processes such as transcription and replication.

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Structural and Functional Features of Bacterial SMC Complexes

Morozova,

Potysyeva,

Vedyaykin

2023

Citologiâ

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SMC complexes (Structural maintenance of chromosomes) are key participants in the spatial organization of DNA in all living organisms – in bacteria, archaea and eukaryotes. In bacteria, there are several homologues of SMC complexes that perform seemingly unrelated functions, but function through very similar, highly conserved mechanisms. In recent years, it has been established that SMC complexes are capable of forming loops from DNA (through the so-called loop extrusion), which allows them to be considered as a separate class of DNA translocases. This paper discusses bacterial SMC complexes in comparison with their homologues such as MukBEF, MksBEF, RecN, and Wadjet, as well as with eukaryotic SMC complexes. Their properties, role and functions in the key processes of the bacterial cell are discussed.

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DNA sliding and loop formation by E. coli SMC complex: MukBEF

Cited by 3 publications

References 68 publications

Properties of theUreaplasma parvumSMC protein related to its interaction with DNA

Properties of theUreaplasma parvumSMC protein related to its interaction with DNA

Spatio-temporal organization of the E. coli chromosome from base to cellular length scales

Structural and Functional Features of Bacterial SMC Complexes

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