MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
The Escherichia coli SMC complex, MukBEF, acts in chromosome segregation. MukBEF shares the distinctive architecture of other SMC complexes, with one prominent difference; unlike other kleisins, MukF forms dimers through its N-terminal domain.
Katarzyna Zawadzka +6 more
doaj +6 more sources
Transient growth arrest in Escherichia coli induced by chromosome condensation. [PDF]
MukB is a bacterial SMC (structural maintenance of chromosome) protein that regulates the global folding of the Escherichia coli chromosome by bringing distant DNA segments together.
Andrea L Edwards +4 more
doaj +3 more sources
Structural basis for the MukB‐topoisomerase IV interaction and its functional implications in vivo [PDF]
Chromosome partitioning in Escherichia coli is assisted by two interacting proteins, topoisomerase (topo) IV and MukB. MukB stimulates the relaxation of negative supercoils by topo IV; to understand the mechanism of their action and to define this functional interplay, we determined the crystal structure of a minimal MukB-topo IV complex to 2.3 Å ...
Seychelle M, Vos +3 more
openaire +3 more sources
Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction [PDF]
In contrast to the current state of knowledge in the field of eukaryotic chromosome segregation, relatively little is known about the mechanisms coordinating the appropriate segregation of bacterial chromosomes. In Escherichia coli , the MukB/E/F complex and topoisomerase IV (Topo IV) are ...
Yinyin, Li +7 more
openaire +3 more sources
Physical and functional interaction between the condensin MukB and the decatenase topoisomerase IV in Escherichia coli [PDF]
Proper geometric and topological organization of DNA is essential for all chromosomal processes. Two classes of proteins play major roles in organizing chromosomes: condensin complexes and type II topoisomerases. In Escherichia coli , MukB, a structural maintenance of chromosome-like ...
Ryo, Hayama, Kenneth J, Marians
openaire +3 more sources
SecA defects are accompanied by dysregulation of MukB, DNA gyrase, chromosome partitioning and DNA superhelicity in Escherichia coli [PDF]
Spatial regulation of nucleoids and chromosome-partitioning proteins is important for proper chromosome partitioning inEscherichia coli. However, the underlying molecular mechanisms are unknown. In the present work, we showed that mutation or chemical perturbation of secretory A (SecA), an ATPase component of the membrane protein translocation ...
Adachi, Shun +2 more
openaire +3 more sources
AbstractThe structural maintenance of chromosomes (SMC) family proteins are commonly found in the multiprotein complexes involved in chromosome organization, including chromosome condensation and sister chromatid cohesion. These proteins are characterized by forming a V‐shaped homo‐ or heterodimeric structure with two long coiled‐coil arms having two ...
Ku, B +4 more
openaire +4 more sources
Dynamic nature of SecA and its associated proteins in Escherichia coli. [PDF]
Mechanical properties such as physical constraint and pushing of chromosomes are thought to be important for chromosome segregation in Escherichia coli and it could be mediated by a hypothetical molecular tether.
Shun eAdachi +4 more
doaj +2 more sources
Author response: MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin [PDF]
The Escherichia coli SMC complex, MukBEF, acts in chromosome segregation. MukBEF shares the distinctive architecture of other SMC complexes, with one prominent difference; unlike other kleisins, MukF forms dimers through its N-terminal domain.
Katarzyna Zawadzka +6 more
openaire +2 more sources
The condensin II complex mutations R551P, R551S, and S556F cause genomic instability by causing DNA damage, anaphase defects, micronuclei, and chromosomal instability. DNA damage and anaphase defects are caused primarily by ataxia telangiectasia and Rad3‐related‐dependent telomere dysfunction.
Emily Weyburne, Giovanni Bosco
wiley +1 more source

