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Escherichia coli K-12 substr. MG1655 Protein: bacterial condensin MukBEF

Subunit composition of bacterial condensin MukBEF = [(MukB)2][(MukE)4([MukF]2)]
         cell division protein involved in chromosome partitioning = (MukB)2
                 cell division protein involved in chromosome partitioning = MukB
         MukEF complex = (MukE)4([MukF]2) (summary available)
                 protein involved in chromosome partitioning = MukE (extended summary available)
                 MukF dimer = (MukF)2
                         Ca2+-binding protein involved in chromosome partitioning = MukF

Summary:
Two conformations of the MukBEF complex appear to exist; the half-saturated complex, with a stoichiometry of B2(E2F)1, is relatively stable and can bind DNA, while the fully saturated MukBEF complex, with a stoichiometry of B2(E2F)2, is short-lived, unable to bind DNA and able to form multimeric complexes [Petrushenko06].

The MukEF complex appears to compete with DNA for binding to MukB. The fully assembled MukBEF complex is unable to bind DNA; addition of MukEF to DNA-bound MukB displaces MukB from the DNA [Petrushenko06].

Electron microscopy studies indicated that the MukE and MukF subunits of the MukBEF complex associate with the terminal globular domains of the MukB homodimer. The MukBEF complex can also be observed to form multimeric complexes in a variety of conformations [Matoba05].

It was reported that he MukBEF complex can be detected in vitro only under conditions of increased Ca2+ or Mg2+ concentration [Yamazoe99]; however, [Matoba05] was able to purify the complex in the absence of ions.

A report that the MukBEF complex was able to compact a DNA molecule in an ATP binding-dependent manner [Case04] was later retracted [Case05].

Review: [Carter12]

Gene-Reaction Schematic: ?


Subunit of bacterial condensin MukBEF: cell division protein involved in chromosome partitioning

Gene: mukB Accession Numbers: EG10618 (EcoCyc), b0924, ECK0915

Locations: cytosol, bacterial nucleoid

Subunit composition of cell division protein involved in chromosome partitioning = [MukB]2
         cell division protein involved in chromosome partitioning = MukB

Map Position: [975,549 -> 980,009] (21.03 centisomes)
Length: 4461 bp / 1486 aa

Molecular Weight of Polypeptide: 170.23 kD (from nucleotide sequence)

Molecular Weight of Multimer: 365.0 kD (experimental) [Niki92]

GO Terms:

Biological Process: GO:0007059 - chromosome segregation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Kruse03, Niki91, Danilova07, Adachi05]
GO:0007062 - sister chromatid cohesion Inferred from experiment [Kruse03]
GO:0030261 - chromosome condensation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Cui08, Wang06f]
GO:0051301 - cell division Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Niki91]
GO:0006260 - DNA replication Inferred by computational analysis [GOA06]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003677 - DNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Niki92]
GO:0005515 - protein binding Inferred from experiment [Vos13, Butland05, Hayama10, Li10c, Lockhart98, Yamazoe99]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Niki92]
GO:0005525 - GTP binding Inferred from experiment [Niki92]
GO:0042802 - identical protein binding Inferred from experiment [Niki92]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0000796 - condensin complex Inferred from experiment [Wang06f]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0009295 - nucleoid Inferred by computational analysis [UniProtGOA11, GOA01a]

MultiFun Terms: cell processes cell division

Unification Links: DIP:DIP-10273N , EcoliWiki:b0924 , Mint:MINT-1225884 , ModBase:P22523 , PR:PRO_000023309 , Pride:P22523 , Protein Model Portal:P22523 , RefSeq:NP_415444 , SMR:P22523 , String:511145.b0924 , UniProt:P22523

Relationship Links: InterPro:IN-FAMILY:IPR007406 , InterPro:IN-FAMILY:IPR012090 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1QHL , PDB:Structure:2WMM , PDB:Structure:3IBP , Pfam:IN-FAMILY:PF04310

Summary:
The MukB protein is involved in chromosome condensation and partitioning. It belongs to the family of SMC (Structural Maintenance of Chromosomes) proteins [Soppa01]. MukB acts as a macromolecular clamp that compacts DNA; condensation is cooperative, and ATP stimulates its initiation, but not propagation [Cui08]. In single-molecule observations, both MukB alone and the MukBEF complex promote shrinkage of large DNA molecules in the presence of ATP [Chen08a].

GFP-marked MukB protein is observed to occupy the same location as the nucleoid in the presence of MukE and MukF [Ohsumi01], and fluorescent antibodies also show localization to the nucleoid, but no colocalization with the FtsZ ring [denBlaauwen01]. In vivo, MukEF is required for association of MukB with the nucleoid [She07]. Mutations in the MukF linker region affect localization of MukB [Shin09c]. MukB generally colocalizes with the origin of replication (oriC) throughout the cell cylce [Danilova07], although the number of MukB foci is larger than the number of oriC foci [Adachi08a]. The oriC region is aberrantly positioned at the cell pole in a mukB mutant [Danilova07]. Sister chromatid interactions are not significantly affected in a mukB mutant [Lesterlin12].

The MukB protein forms a homodimer [Niki92]. Like other members of the SMC protein family, MukB is a large protein made up of five domains: N- and C-terminal globular "head domains", a central linker region or "hinge domain", and two coiled-coil rod domains that separate the head domains from the hinge domain. This structure can be visualized by EM; the coiled-coil regions are arranged in an antiparallel fashion in the homodimer [Melby98, Matoba05]. The relative alignment of the N- and C-terminal halves of the coiled-coil region has been investigated by site-directed crosslinking [Li09c]. Interacting pairs of residues were identified by disulfide crosslinking, revealing that five coiled-coil segments are interrupted by a novel structural motif, called a coiled-coil knuckle [Weitzel11a].

The C-terminal region of MukB is essential for its DNA binding activity [Niki92, Saleh96], while the hinge domain does not appear to interact with DNA [Ku10]. ATP is not required for DNA binding [Petrushenko06a]. A purified N-terminal domain of MukB binds to FtsZ in vitro [Lockhart98]. A crystal structure of the 227 N-terminal amino acid residues of MukB has been solved at 2.2 Å resolution [vandenEnt99]. Crystal structures of the central hinge domain responsible for dimerization of MukB, including a portion of the adjacent coiled-coil domain, have been solved at 3.1 and 2.3 Å resolution [Li10d, Ku10]. The hinge domain interacts directly with the C-terminal domain of ParC and stimulates the DNA relaxation and knotting activities of topoisomerase IV in vitro [Hayama10, Li10c, Hayama13], but not its decatenation activity [Hayama13]. The crystal structure of a minimal MukB-topo IV complex has been solved; the MukB hinge domain is shown to stimulate topo IV by competing for a site on its C-terminal domain that normally represses activity on negatively supercoiled DNA [Vos13].

A mukB null mutant has a cell division defect and can not form colonies [Niki91]. mukB mutants are temperature sensitive and produce anucleate cells. A mukB mutation causes unfolding of the nucleoid; this phenotype is supressed by a mutation in seqA [Weitao99, Onogi00]. Additional supressors of the mukB null mutant phenotype have been isolated in smbA [Yamanaka92], msmA, msmB, msmC [Yamanaka94], smbB [Kido96], crcA, cspE, crcB [Hu96a], topA [Sawitzke00], and gyrB [Adachi03b]. In a mukB mutant, the chromosome appears to be less supercoiled [Weitao00]. Overproduction of MukB leads to condensation of chromosomes, even in the absence of MukE and MukF [Wang06f].

Reviews: [Luijsterburg06, Graumann09, Hirano10]

Gene Citations: [Yamanaka95, Yamanaka96]

Essentiality data for mukB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of bacterial condensin MukBEF: MukEF complex

Molecular Weight: 230.0 kD (experimental) [Petrushenko06]

Summary:
The MukEF complex is asymmetric and likely has an elongated shape [Petrushenko06]. An intermediate complex with 2:2 stiochiometry of MukE and MukF has also been observed; in vivo experiments suggest the presence of nearly equimolar amounts of F2E2 and F2E4 [Gloyd07].


Subunit of MukEF complex: protein involved in chromosome partitioning

Synonyms: YcbA, KicA, MukE

Gene: mukE Accession Numbers: EG11252 (EcoCyc), b0923, ECK0914

Locations: cytosol, bacterial nucleoid

Sequence Length: 225 AAs

Molecular Weight: 25.984 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006260 - DNA replication Inferred by computational analysis [GOA06]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
GO:0007059 - chromosome segregation Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0030261 - chromosome condensation Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0051301 - cell division Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Woo09, Butland05, Oishi06]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0009295 - nucleoid Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes cell division
cell processes defense/survival
information transfer DNA related
regulation type of regulation unknown

Unification Links: DIP:DIP-10274N , EcoliWiki:b0923 , Mint:MINT-1227862 , PR:PRO_000023310 , Protein Model Portal:P22524 , RefSeq:NP_415443 , SMR:P22524 , String:511145.b0923 , UniProt:P22524

Relationship Links: InterPro:IN-FAMILY:IPR007385 , PDB:Structure:3EUH , PDB:Structure:3RPU , Pfam:IN-FAMILY:PF04288

Summary:
MukE plays a role in chromosome partitioning during cell division [Yamanaka96]. The effect of MukE on chromosome partitioning may be due to a role in DNA topology or condensation [Sawitzke00]. MukF and MukE are proposed to be a toxin-antitoxin pair, respectively [Feng94].

Published reports disagree about whether [Feng94] or not [Yamanaka96] MukE is essential for viability. A mukE mutant is reported to exhibit heat sensitivity and formation of anucleate products of cell division [Yamanaka96]. A mukE mutant also exhibits increased sensitivity to novobiocin, compared to wild type [Onogi00]. A mukE mutant exhibits a defect in wild-type localization of MukB to nucleoid-associated foci [Ohsumi01]. A mukF mutation suppresses the observed inviability of a mukE mutant [Feng94]. The heat sensitivity and division defects of a mukE mutant are suppressed by a topA10 or topA66 mutation, and this suppression is DNA gyrase dependent [Sawitzke00]. The heat sensitivity of a mukE mutant is partly suppressed by a dam or seqA mutation, whereas the novobiocin and anucleate cell phenotypes are not [Onogi00].

Loss-of-function point mutations in MukE affect focal localization of the MukBEF complex in vivo [She13].

MukB, MukE and MukF form a complex; MukE binding to MukB requires MukF, whereas MukF binding to MukB does not require MukE, and complex formation is stimulated by Ca2+ or Mg2+ [Yamazoe99].

KicA: killing of cell A [Feng94]

Regulation has been described [Feng94, Yamanaka95].

Citations: [Gloyd11]

Essentiality data for mukE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of MukEF complex: MukF dimer

Synonyms: kicB

Gene: mukF Accession Numbers: EG12165 (EcoCyc), b0922, ECK0913

Locations: cytosol, bacterial nucleoid

Subunit composition of MukF dimer = [MukF]2
         Ca2+-binding protein involved in chromosome partitioning = MukF

Map Position: [973,542 -> 974,864] (20.98 centisomes)
Length: 1323 bp / 440 aa

Molecular Weight of Polypeptide: 50.579 kD (from nucleotide sequence)

Molecular Weight of Multimer: 105.0 kD (experimental) [Gloyd07]

GO Terms:

Biological Process: GO:0006260 - DNA replication Inferred by computational analysis [GOA06, GOA01a]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
GO:0007059 - chromosome segregation Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0030261 - chromosome condensation Inferred by computational analysis [UniProtGOA11a]
GO:0051301 - cell division Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Woo09, Butland05, Oishi06]
GO:0005509 - calcium ion binding Inferred by computational analysis [GOA06, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0009295 - nucleoid Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes cell division
cell processes protection cell killing
information transfer DNA related

Unification Links: DIP:DIP-39981N , EcoliWiki:b0922 , Mint:MINT-1300138 , PR:PRO_000023311 , Pride:P60293 , Protein Model Portal:P60293 , RefSeq:NP_415442 , SMR:P60293 , String:511145.b0922 , UniProt:P60293

Relationship Links: InterPro:IN-FAMILY:IPR005582 , InterPro:IN-FAMILY:IPR011991 , PDB:Structure:1T98 , PDB:Structure:3EUH , PDB:Structure:3RPU , Pfam:IN-FAMILY:PF03882

Summary:
MukF plays a role in chromosome partitioning during cell division [Yamanaka96]. The effect of MukF on chromosome partitioning may be due to a role in DNA topology or condensation [Sawitzke00]. MukF and MukE are proposed to be a toxin-antitoxin pair, respectively [Feng94].

A mukF mutant is viable [Feng94]. A mukF mutant is reported to exhibit heat sensitivity and formation of anucleate products of cell division [Yamanaka96]. A mukF mutant also exhibits increased sensitivity to novobiocin, compared to wild type [Onogi00]. A mukF mutant exhibits a defect in wild-type localization of MukB to nucleoid-associated foci [Ohsumi01]. Like a mukF mutation, MukF overproduction results in a cell division defect with anucleate cells [Yamanaka96]. A mukF mutation suppresses the viability defect of a mukE mutant [Feng94]. The heat sensitivity and division defects of a mukF mutant are suppressed by a topA10 or topA66 mutation, and this suppression is DNA gyrase dependent [Sawitzke00]. The heat sensitivity of a mukF mutant is partly suppressed by a dam or seqA mutation, whereas the novobiocin and anucleate cell phenotypes are not [Onogi00].

MukF has a leucine zipper region and an acidic region; both regions are functionally important [Yamanaka96]. MukF binds Ca2+ [Yamazoe99].

MukB, MukE and MukF form a complex; MukE binding to MukB requires MukF, whereas MukF binding to MukB does not require MukE, and complex formation is stimulated by Ca2+ or Mg2+ [Yamazoe99].

KicB: "killing of cell" [Feng94].

Regulation has been described [Feng94, Yamanaka95].

Essentiality data for mukF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

References

Adachi03b: Adachi S, Hiraga S (2003). "Mutants suppressing novobiocin hypersensitivity of a mukB null mutation." J Bacteriol 185(13);3690-5. PMID: 12813060

Adachi05: Adachi S, Kohiyama M, Onogi T, Hiraga S (2005). "Localization of replication forks in wild-type and mukB mutant cells of Escherichia coli." Mol Genet Genomics 274(3);264-71. PMID: 16133165

Adachi08a: Adachi S, Fukushima T, Hiraga S (2008). "Dynamic events of sister chromosomes in the cell cycle of Escherichia coli." Genes Cells 13(2);181-97. PMID: 18233960

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Carter12: Carter SD, Sjogren C (2012). "The SMC complexes, DNA and chromosome topology: right or knot?." Crit Rev Biochem Mol Biol 47(1);1-16. PMID: 21923481

Case04: Case RB, Chang YP, Smith SB, Gore J, Cozzarelli NR, Bustamante C (2004). "The bacterial condensin MukBEF compacts DNA into a repetitive, stable structure." Science 305(5681);222-7. PMID: 15178751

Case05: Case RB, Chang YP, Smith SB, Gore J, Cozzarelli NR, Bustamante C (2005). "Retraction." Science 307(5714);1409. PMID: 15746408

Chen08a: Chen N, Zinchenko AA, Yoshikawa Y, Araki S, Adachi S, Yamazoe M, Hiraga S, Yoshikawa K (2008). "ATP-induced shrinkage of DNA with MukB protein and the MukBEF complex of Escherichia coli." J Bacteriol 190(10);3731-7. PMID: 18326568

Cui08: Cui Y, Petrushenko ZM, Rybenkov VV (2008). "MukB acts as a macromolecular clamp in DNA condensation." Nat Struct Mol Biol 15(4);411-8. PMID: 18376412

Danilova07: Danilova O, Reyes-Lamothe R, Pinskaya M, Sherratt D, Possoz C (2007). "MukB colocalizes with the oriC region and is required for organization of the two Escherichia coli chromosome arms into separate cell halves." Mol Microbiol 65(6);1485-92. PMID: 17824928

denBlaauwen01: den Blaauwen T, Lindqvist A, L?we J, Nanninga N (2001). "Distribution of the Escherichia coli structural maintenance of chromosomes (SMC)-like protein MukB in the cell." Mol Microbiol 42(5);1179-88. PMID: 11886550

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feng94: Feng J, Yamanaka K, Niki H, Ogura T, Hiraga S (1994). "New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coli." Mol Gen Genet 243(2);136-47. PMID: 7513784

Gloyd07: Gloyd M, Ghirlando R, Matthews LA, Guarne A (2007). "MukE and MukF form two distinct high affinity complexes." J Biol Chem 282(19);14373-8. PMID: 17355972

Gloyd11: Gloyd M, Ghirlando R, Guarne A (2011). "The role of MukE in assembling a functional MukBEF complex." J Mol Biol 412(4);578-90. PMID: 21855551

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Graumann09: Graumann PL, Knust T (2009). "Dynamics of the bacterial SMC complex and SMC-like proteins involved in DNA repair." Chromosome Res 17(2);265-75. PMID: 19308706

Hayama10: Hayama R, Marians KJ (2010). "Physical and functional interaction between the condensin MukB and the decatenase topoisomerase IV in Escherichia coli." Proc Natl Acad Sci U S A 107(44);18826-31. PMID: 20696938

Hayama13: Hayama R, Bahng S, Karasu ME, Marians KJ (2013). "The MukB-ParC interaction affects the intramolecular, not intermolecular, activities of topoisomerase IV." J Biol Chem 288(11);7653-61. PMID: 23349462

Hirano10: Hirano T (2010). "How to separate entangled sisters: interplay between condensin and decatenase." Proc Natl Acad Sci U S A 107(44);18749-50. PMID: 20962275

Hu96a: Hu KH, Liu E, Dean K, Gingras M, DeGraff W, Trun NJ (1996). "Overproduction of three genes leads to camphor resistance and chromosome condensation in Escherichia coli." Genetics 143(4);1521-32. PMID: 8844142

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kido96: Kido M, Yamanaka K, Mitani T, Niki H, Ogura T, Hiraga S (1996). "RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli." J Bacteriol 178(13);3917-25. PMID: 8682798

Kruse03: Kruse T, Moller-Jensen J, Lobner-Olesen A, Gerdes K (2003). "Dysfunctional MreB inhibits chromosome segregation in Escherichia coli." EMBO J 22(19);5283-92. PMID: 14517265

Ku10: Ku B, Lim JH, Shin HC, Shin SY, Oh BH (2010). "Crystal structure of the MukB hinge domain with coiled-coil stretches and its functional implications." Proteins 78(6);1483-90. PMID: 20034111

Lesterlin12: Lesterlin C, Gigant E, Boccard F, Espeli O (2012). "Sister chromatid interactions in bacteria revealed by a site-specific recombination assay." EMBO J 31(16);3468-79. PMID: 22820946

Li09c: Li Y, Weitzel CS, Arnold RJ, Oakley MG (2009). "Identification of interacting regions within the coiled coil of the Escherichia coli structural maintenance of chromosomes protein MukB." J Mol Biol 391(1);57-73. PMID: 19482037

Li10c: Li Y, Stewart NK, Berger AJ, Vos S, Schoeffler AJ, Berger JM, Chait BT, Oakley MG (2010). "Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction." Proc Natl Acad Sci U S A 107(44);18832-7. PMID: 20921377

Li10d: Li Y, Schoeffler AJ, Berger JM, Oakley MG (2010). "The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB." J Mol Biol 395(1);11-9. PMID: 19853611

Lockhart98: Lockhart A, Kendrick-Jones J (1998). "Interaction of the N-terminal domain of MukB with the bacterial tubulin homologue FtsZ." FEBS Lett 430(3);278-82. PMID: 9688555

Luijsterburg06: Luijsterburg MS, Noom MC, Wuite GJ, Dame RT (2006). "The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: a molecular perspective." J Struct Biol 156(2);262-72. PMID: 16879983

Matoba05: Matoba K, Yamazoe M, Mayanagi K, Morikawa K, Hiraga S (2005). "Comparison of MukB homodimer versus MukBEF complex molecular architectures by electron microscopy reveals a higher-order multimerization." Biochem Biophys Res Commun 333(3);694-702. PMID: 15979051

Melby98: Melby TE, Ciampaglio CN, Briscoe G, Erickson HP (1998). "The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge." J Cell Biol 142(6);1595-604. PMID: 9744887

Niki91: Niki H, Jaffe A, Imamura R, Ogura T, Hiraga S (1991). "The new gene mukB codes for a 177 kd protein with coiled-coil domains involved in chromosome partitioning of E. coli." EMBO J 10(1);183-93. PMID: 1989883

Niki92: Niki H, Imamura R, Kitaoka M, Yamanaka K, Ogura T, Hiraga S (1992). "E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities." EMBO J 11(13);5101-9. PMID: 1464330

Ohsumi01: Ohsumi K, Yamazoe M, Hiraga S (2001). "Different localization of SeqA-bound nascent DNA clusters and MukF-MukE-MukB complex in Escherichia coli cells." Mol Microbiol 40(4);835-45. PMID: 11401691

Oishi06: Oishi Y, Yunomura S, Kawahashi Y, Doi N, Takashima H, Baba T, Mori H, Yanagawa H (2006). "Escherichia coli proteome chips for detecting protein-protein interactions." Proteomics 6(24);6433-6. PMID: 17109382

Onogi00: Onogi T, Yamazoe M, Ichinose C, Niki H, Hiraga S (2000). "Null mutation of the dam or seqA gene suppresses temperature-sensitive lethality but not hypersensitivity to novobiocin of muk null mutants." J Bacteriol 182(20);5898-901. PMID: 11004192

Petrushenko06: Petrushenko ZM, Lai CH, Rybenkov VV (2006). "Antagonistic interactions of kleisins and DNA with bacterial Condensin MukB." J Biol Chem 281(45);34208-17. PMID: 16982609

Petrushenko06a: Petrushenko ZM, Lai CH, Rai R, Rybenkov VV (2006). "DNA reshaping by MukB. Right-handed knotting, left-handed supercoiling." J Biol Chem 281(8);4606-15. PMID: 16368697

Saleh96: Saleh AZ, Yamanaka K, Niki H, Ogura T, Yamazoe M, Hiraga S (1996). "Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity." FEMS Microbiol Lett 143(2-3);211-6. PMID: 8837474

Sawitzke00: Sawitzke JA, Austin S (2000). "Suppression of chromosome segregation defects of Escherichia coli muk mutants by mutations in topoisomerase I." Proc Natl Acad Sci U S A 97(4);1671-6. PMID: 10660686

She07: She W, Wang Q, Mordukhova EA, Rybenkov VV (2007). "MukEF Is required for stable association of MukB with the chromosome." J Bacteriol 189(19);7062-8. PMID: 17644586

She13: She W, Mordukhova E, Zhao H, Petrushenko ZM, Rybenkov VV (2013). "Mutational analysis of MukE reveals its role in focal subcellular localization of MukBEF." Mol Microbiol 87(3);539-52. PMID: 23171168

Shin09c: Shin HC, Lim JH, Woo JS, Oh BH (2009). "Focal localization of MukBEF condensin on the chromosome requires the flexible linker region of MukF." FEBS J 276(18);5101-10. PMID: 19674109

Soppa01: Soppa J (2001). "Prokaryotic structural maintenance of chromosomes (SMC) proteins: distribution, phylogeny, and comparison with MukBs and additional prokaryotic and eukaryotic coiled-coil proteins." Gene 278(1-2);253-64. PMID: 11707343

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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