Antagonistic Interactions of Kleisins and DNA with Bacterial Condensin MukB

MukBEF is a bacterial SMC (structural maintenance of chromosome) complex required for faithful chromosome segregation in Escherichia coli. The SMC subunit of the complex, MukB, promotes DNA condensation in vitro and in vivo; however, all three subunits are required for the function of MukBEF. We report here that MukEF disrupts MukB·DNA complex. Preassembled MukBEF was inert in DNA binding or reshaping. Similarly, the association of MukEF with DNA-bound MukB served to displace MukB from DNA. When purified from cells, MukBEF existed as a mixture of MukEF-saturated and unsaturated complexes. The holoenzyme was unstable and could only bind DNA upon dissociation of MukEF. The DNA reshaping properties of unsaturated MukBEF were identical to those of MukB. Furthermore, the unsaturated MukBEF was stable and proficient in DNA binding. These results support the view that kleisins are not directly involved in DNA binding but rather bridge distant DNA-bound MukBs. MukBEF is a bacterial SMC (structural maintenance of chromosome) complex required for faithful chromosome segregation in Escherichia coli. The SMC subunit of the complex, MukB, promotes DNA condensation in vitro and in vivo; however, all three subunits are required for the function of MukBEF. We report here that MukEF disrupts MukB·DNA complex. Preassembled MukBEF was inert in DNA binding or reshaping. Similarly, the association of MukEF with DNA-bound MukB served to displace MukB from DNA. When purified from cells, MukBEF existed as a mixture of MukEF-saturated and unsaturated complexes. The holoenzyme was unstable and could only bind DNA upon dissociation of MukEF. The DNA reshaping properties of unsaturated MukBEF were identical to those of MukB. Furthermore, the unsaturated MukBEF was stable and proficient in DNA binding. These results support the view that kleisins are not directly involved in DNA binding but rather bridge distant DNA-bound MukBs. SMCs are ubiquitous highly conserved proteins that have been implicated in virtually every aspect of higher order chromatin dynamics. Eukaryotic cells contain at least six different SMC complexes with functions in chromosome condensation and segregation, recombination, and repair (1Swedlow J.R. Hirano T. Mol. Cell. 2003; 11: 557-569Abstract Full Text Full Text PDF PubMed Scopus (226) Google Scholar, 2Cobbe N. Heck M.M. J. Struct. Biol. 2000; 129: 123-143Crossref PubMed Scopus (114) Google Scholar, 3Nasmyth K. Haering C.H. Annu. Rev. Biochem. 2005; 74: 595-648Crossref PubMed Scopus (497) Google Scholar, 4Koshland D. Strunnikov A. Annu. Rev. Cell Dev. Biol. 1996; 12: 305-333Crossref PubMed Scopus (286) Google Scholar). Bacteria carry two SMC complexes. In Escherichia coli, faithful chromosome segregation requires the action of MukBEF (5Hiraga S. Annu. Rev. Genet. 2000; 34: 21-59Crossref PubMed Scopus (134) Google Scholar, 6Sherratt D.J. Science. 2003; 301: 780-785Crossref PubMed Scopus (163) Google Scholar). The second SMC complex, SbcCD nuclease, was implicated in the metabolism of double-strand DNA breaks (7Connelly J.C. de Leau E.S. Leach D.R. DNA Repair (Amst.). 2003; 2: 795-807Crossref PubMed Scopus (80) Google Scholar). The defining feature of SMCs is their structure. They consist of two globular domains connected by a long coil-hinge-coil motif. In solution, SMCs dimerize to form an idiosyncratic V-shaped structure with two globular head domains connected at the hinge via two long coiled coils (8Melby T.E. Ciampaglio C.N. Briscoe G. Erickson H.P. J. Cell Biol. 1998; 142: 1595-1604Crossref PubMed Scopus (332) Google Scholar, 9Anderson D.E. Losada A. Erickson H.P. Hirano T. J. Cell Biol. 2002; 156: 419-424Crossref PubMed Scopus (298) Google Scholar, 10Haering C.H. Lowe J. Hochwagen A. Nasmyth K. Mol. Cell. 2002; 9: 773-788Abstract Full Text Full Text PDF PubMed Scopus (558) Google Scholar). The Walker A and B motifs, which are found in the N- and C-terminal domains of SMCs, are located at the surface of the SMC heads. This enables further association of SMCs via nucleotide-sandwiched dimerization of the head domains, leading to the formation of protein rings (11Hopfner K.P. Karcher A. Shin D.S. Craig L. Arthur L.M. Carney J.P. Tainer J.A. Cell. 2000; 101: 789-800Abstract Full Text Full Text PDF PubMed Scopus (808) Google Scholar, 12Lammens A. Schele A. Hopfner K.P. Curr. Biol. 2004; 14: 1778-1782Abstract Full Text Full Text PDF PubMed Scopus (120) Google Scholar, 13Arumugam P. Gruber S. Tanaka K. Haering C.H. Mechtler K. Nasmyth K. Curr. Biol. 2003; 13: 1941-1953Abstract Full Text Full Text PDF PubMed Scopus (210) Google Scholar) or macromolecular assemblies (14Hirano M. Hirano T. EMBO J. 2004; 23: 2664-2673Crossref PubMed Scopus (103) Google Scholar, 15Hirano M. Anderson D.E. Erickson H.P. Hirano T. EMBO J. 2001; 20: 3238-3250Crossref PubMed Scopus (141) Google Scholar, 16de Jager M. van Noort J. van Gent D.C. Dekker C. Kanaar R. Wyman C. Mol. Cell. 2001; 8: 1129-1135Abstract Full Text Full Text PDF PubMed Scopus (376) Google Scholar). SMCs act inside the cell as a part of multisubunit complexes. Among the non-SMC subunits, a conserved family of kleisins was identified (17Soppa J. Kobayashi K. Noirot-Gros M.F. Oesterhelt D. Ehrlich S.D. Dervyn E. Ogasawara N. Moriya S. Mol. Microbiol. 2002; 45: 59-71Crossref PubMed Scopus (103) Google Scholar, 18Schleiffer A. Kaitna S. Maurer-Stroh S. Glotzer M. Nasmyth K. Eisenhaber F. Mol. Cell. 2003; 11: 571-575Abstract Full Text Full Text PDF PubMed Scopus (183) Google Scholar). Kleisins bind head domains in the vicinity of the ATP binding site and apparently stabilize the dimeric form of the SMC heads (11Hopfner K.P. Karcher A. Shin D.S. Craig L. Arthur L.M. Carney J.P. Tainer J.A. Cell. 2000; 101: 789-800Abstract Full Text Full Text PDF PubMed Scopus (808) Google Scholar, 19Haering C.H. Schoffnegger D. Nishino T. Helmhart W. Nasmyth K. Lowe J. Mol. Cell. 2004; 15: 951-964Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar, 20Uhlmann F. Wernic D. Poupart M.A. Koonin E.V. Nasmyth K. Cell. 2000; 103: 375-386Abstract Full Text Full Text PDF PubMed Scopus (648) Google Scholar). In several cases, a functional interaction between kleisins and ATP has been reported (11Hopfner K.P. Karcher A. Shin D.S. Craig L. Arthur L.M. Carney J.P. Tainer J.A. Cell. 2000; 101: 789-800Abstract Full Text Full Text PDF PubMed Scopus (808) Google Scholar, 14Hirano M. Hirano T. EMBO J. 2004; 23: 2664-2673Crossref PubMed Scopus (103) Google Scholar, 21Weitzer S. Lehane C. Uhlmann F. Curr. Biol. 2003; 13: 1930-1940Abstract Full Text Full Text PDF PubMed Scopus (168) Google Scholar). Biochemical properties of SMCs befit their intracellular functions. In a reaction coupled to type-2 DNA topoisomerases, condensins promote formation of DNA knots of specific topology (22Kimura K. Rybenkov V. Crisona N. Hirano T. Cozzarelli N. Cell. 1999; 98: 239-248Abstract Full Text Full Text PDF PubMed Scopus (267) Google Scholar, 23Stray J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar, 24Petrushenko Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). This is highly conserved condensins and DNA In promote DNA DNA A. Hirano T. Curr. Biol. 2001; 11: Full Text Full Text PDF PubMed Scopus Google Scholar). the condensins and between their The of SMCs is were to the of DNA reshaping (1Swedlow J.R. Hirano T. Mol. Cell. 2003; 11: 557-569Abstract Full Text Full Text PDF PubMed Scopus (226) Google Scholar, 23Stray J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar, 24Petrushenko Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The for that the proteins DNA via a (1Swedlow J.R. Hirano T. Mol. Cell. 2003; 11: 557-569Abstract Full Text Full Text PDF PubMed Scopus (226) Google Scholar, 10Haering C.H. Lowe J. Hochwagen A. Nasmyth K. Mol. Cell. 2002; 9: 773-788Abstract Full Text Full Text PDF PubMed Scopus (558) Google Scholar). least for is at with the binding of the proteins to DNA and the of knots (22Kimura K. Rybenkov V. Crisona N. Hirano T. Cozzarelli N. Cell. 1999; 98: 239-248Abstract Full Text Full Text PDF PubMed Scopus (267) Google Scholar, 23Stray J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar, 24Petrushenko Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). A in the of SMCs is the of kleisins in DNA reshaping. The with from that the non-SMC subunits and ATP are required for DNA but not for DNA binding K. Hirano T. S. A. 2000; PubMed Scopus (120) Google Scholar). This with which for in SMC and non-SMC of the complex, and the that the of kleisins to of between F. Wernic D. Poupart M.A. Koonin E.V. Nasmyth K. Cell. 2000; 103: 375-386Abstract Full Text Full Text PDF PubMed Scopus (648) Google Scholar). In the complex and the E. MukB protein promote DNA in the of ATP and the subunits J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar, 24Petrushenko Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). with the SMC complex that the subunits the association of the protein with DNA (14Hirano M. Hirano T. EMBO J. 2004; 23: 2664-2673Crossref PubMed Scopus (103) Google Scholar). however, the of the holoenzyme the DNA reshaping properties of the the of the non-SMC subunits in DNA reshaping by bacterial MukB R. M. K. T. S. EMBO J. 11: PubMed Scopus Google Scholar). In complex with MukB the in the chromosome of E. (5Hiraga S. Annu. Rev. Genet. 2000; 34: 21-59Crossref PubMed Scopus (134) Google Scholar). of MukBEF results in the of cell chromosome and and a of cells K. T. S. Mol. Genet. 1996; Google Scholar). The of MukBEF to the that a in the of the Rybenkov V.V. J. PubMed Scopus Google Scholar). the function of MukBEF to chromosome is by that DNA J.A. S. S. A. 2000; PubMed Scopus Google Scholar, T. K. S. Mol. Microbiol. 1999; 34: PubMed Scopus Google to the structure of highly Cozzarelli N.R. S. A. 2000; PubMed Scopus Google Scholar, V.V. Cozzarelli N.R. J. Mol. Biol. PubMed Scopus Google Scholar). as a between MukB and M. T. K. T. S. EMBO J. 1999; PubMed Scopus Google Scholar). via and with MukB or M. T. K. T. S. EMBO J. 1999; PubMed Scopus Google Scholar, R. S.D. D. EMBO J. 2005; PubMed Scopus Google Scholar). A that is a R. S.D. D. EMBO J. 2005; PubMed Scopus Google Scholar). but not MukB, was found to form and in the of ATP or DNA K. M. K. K. S. Biochem. 2005; PubMed Scopus Google Scholar). MukB and DNA with MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google and bind ATP and in the of R. M. K. T. S. EMBO J. 11: PubMed Scopus Google Scholar). The of MukB is the reported for the SMC proteins and is not by or DNA Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The however, DNA in the of ATP or and promotes formation of the of condensins Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). the MukB but to the of cells Rybenkov V.V. J. PubMed Scopus Google Scholar). the subunits of MukBEF to for DNA but are required for of chromosome We report here that MukEF has only DNA reshaping. Preassembled MukBEF was to bind or DNA binding with the of the The interaction of MukEF with DNA-bound MukB served to displace MukB from DNA. MukEF and DNA for binding to MukB. We however, that only of were the complexes were in the of MukBEF is to act inside the cell as an We found that the MukBEF DNA reshaping. Furthermore, a stable complex could at of MukEF. We found properties for MukBEF that was purified from MukBEF existed as a mixture of two of which was unsaturated with MukEF. The MukEF-saturated MukBEF was unstable and the DNA binding dissociation of MukEF. The MukBEF was from MukB in DNA binding and reshaping. These support the view that DNA binding and reshaping is by the SMC subunit of the complex, kleisins are for of chromosome were Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). and which C-terminal MukB or were purified from cells or Rybenkov V.V. J. PubMed Scopus Google Scholar). The of all proteins has been Rybenkov V.V. J. PubMed Scopus Google Scholar). and were purified by a as for MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). the of MukB was was purified by by proteins were found in purified MukEF or the of of to MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google protein not with DNA reshaping the and purified MukEF was in and to the was with was with in the and the proteins were by MukBEF was by MukEF and MukB in by of were as a DNA and were in reaction with and as Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). DNA binding was in reaction or as The were and by at at in or for DNA was by with of MukBEF was with of and in The protein mixture was of in the that was and at for at in The proteins in were by by and was by a and the and of proteins was and The of the proteins was from and The of the that for a of a is and is directly to the of the E. Mol. Biol. Google Scholar). MukEF an with the was purified from cells that and the C-terminal MukEF as a and In with M. T. K. T. S. EMBO J. 1999; PubMed Scopus Google the of MukEF was found to S. The of as by at and at This in MukEF and the of is however, that MukEF is an the for the the of MukEF as which the of W. and Scholar). When E. Mol. Biol. Google the of MukEF was found to This is with two and between the of MukEF two MukEF was to the mixture of purified MukB, and The of and was by the of from the of to was found to the purified and were in and by at a of a the We that the of MukEF is The dimeric of MukEF that the protein with two head domains of MukB, which is with of a of MukB and of MukBEF was by purified MukB and MukEF in the the of of MukB and MukEF were to MukB and MukBEF to the from MukEF found that only of MukEF with MukB the mixture of MukB and MukEF was by in the of This was not of a all MukEF a complex with MukB the proteins were at the of Furthermore, the MukBEF was stable to found of MukEF by MukB protein were to in the of reaction of MukEF with MukB higher of MukEF were in that the of the proteins is to complex formation rather protein The of and the was required for binding of MukB to MukEF. of MukB MukEF at and of MukBEF at not two of complexes are of the MukBEF was the was by and MukBEF a kleisins could the head domains from the or different V-shaped of MukB. or assemblies in two between two MukBEF by the with MukB and MukBEF as the was in the The of the proteins for MukB and for are with the Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, M. T. K. T. S. EMBO J. 1999; PubMed Scopus Google Scholar) and the dimeric MukB at the of MukBEF. The was different in the of In MukB in or to the of the the of the protein In MukBEF in the of the the interaction with MukEF served to MukB MukB and MukEF not in the of the of the This is in with of the association between MukB and MukEF The two only in the for The of which was in could stabilize MukBEF via J.R. 1998; PubMed Scopus Google Scholar). In with the MukEF in mixture the the MukEF This that could MukB and MukEF to the of the at a an of between MukB and MukEF. The of to not association with MukB and the of MukEF-saturated MukBEF is This the that MukB with MukEF via M. T. K. T. S. EMBO J. 1999; PubMed Scopus Google Scholar, R. S.D. D. EMBO J. 2005; PubMed Scopus Google Scholar). however, MukBEF as a rather a The MukBEF to a complex rather an of MukB and MukEF MukEF is in Furthermore, the MukBEF is in the of and higher only the stable MukBEF The MukBEF as a and and not to contain MukB B and the of the MukBEF is the dimeric two upon formation of the MukBEF. Preassembled MukBEF or was to form a stable complex with DNA and promote DNA and in the and Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, R. M. K. T. S. EMBO J. 11: PubMed Scopus Google Scholar). We here the association of MukB and MukEF. MukB was with of and the mixture was in DNA and as for MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). We found in MukBEF with MukB. the of MukBEF all of MukB with DNA. DNA was at a of MukEF were to was from the This is with that the complex is the complex of MukB that are to bind DNA. The DNA binding at of apparently the binding of MukEF to We found a of the and upon formation of the of the of MukEF in a in DNA and of MukB, of MukEF and This is in with the that condensins and and at J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar, 24Petrushenko Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). We found that of MukB DNA by the in further the view that the of MukB upon binding to MukEF. or could the of MukEF that of MukB Similarly, the association with MukEF the of MukB DNA We that the of MukBEF MukB from DNA binding. between MukEF and DNA for to MukEF with DNA-bound MukB. We however, only of MukEF the MukB·DNA complex. or the of DNA was only of with and was the of kleisins In the complex of MukB with DNA was not by long We results complex was in the of only the complex is and complex is to bind DNA The of which in the of DNA from the complex of MukEF were in MukB from DNA only between MukB and MukEF is a of the between MukEF and DNA for binding to MukB. that DNA with the of MukBEF. of the MukEF was to bind MukB in the of the of DNA MukEF and DNA bind MukB a MukBEF a with the between DNA and MukEF was the identical of in MukB, and K. T. S. Mol. Genet. 1996; Google Scholar). We however, that MukB, a act as an with to DNA and the to MukEF. The of has been by the that only of are stable the by of MukB and MukEF with the mixture by dissociation of MukB from was at in reaction MukB MukBEF as a with the of with of MukEF was from the complex, as was found however, MukBEF was found with in the of the We that the MukBEF bind DNA. MukBEF and DNA of that the of MukEF DNA binding was not an of the in vitro MukBEF that was purified from cells that all three subunits of the complex and The complex was purified by of the C-terminal MukB. MukBEF was a MukBEF as two from The the and were in and The not between the two of MukBEF. proteins as and with of MukB or MukEF not The and the for and were as and and as and These with the M. T. K. T. S. EMBO J. 1999; PubMed Scopus Google Scholar) and are with the for the complex. of the however, that is in MukB and MukEF are in The found for and and not A that but not is to bind MukEF In with the the MukEF with only in the of The two of MukBEF in their DNA binding DNA and only in the but not in the of and was inert in DNA and In was in DNA binding and reshaping. The DNA reshaping properties of were highly to those of MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The of knots were with a of the and that by to and Crisona Crisona N.J. Mol. Biol. 1999; Google were The and required between and condensins which is for MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). This is with the of MukB in the of of MukBEF DNA reshaping as was reported for MukB and the complex J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar). We that the are for the DNA reshaping of as a and that protein not contain MukB. the complex between and MukEF was only stable in the of as found for the complex but not for MukB We that DNA reshaping is by rather by MukB. The of MukBEF two could to of the subunits of the complex. the purified MukBEF could between to of The of MukBEF at the higher second The DNA was only found in the the of not with the of the that the MukBEF is not MukBEF from several for the to bind MukEF. We found that the of MukBEF a for MukEF the purified MukBEF is unstable and the to bind and DNA dissociation of MukEF. MukEF in E. only the of DNA binding by MukEF. DNA binding were found in MukB. The complex was stable and proficient in DNA binding and reshaping. MukBEF in cells as a complex, the of all three proteins in E. The of MukB which with an a different M. K. T. T. S. J. 1996; PubMed Google Scholar). The to cell the of the The of and virtually the and MukEF is inside the cell MukB. MukBEF a in the chromosome of E. coli. that all three subunits of the complex are for MukBEF function in K. T. S. Mol. Genet. 1996; Google Scholar). as a found that MukB DNA in vitro and in from MukEF Rybenkov V.V. J. PubMed Scopus Google Scholar). We here that MukEF in disrupts the interaction of MukB with DNA. Preassembled MukBEF was inert in DNA binding and of DNA-bound MukB with MukEF in of MukB from DNA. in with the of that MukEF and DNA for binding to MukB. ATP the of MukBEF or the between MukEF and which is with the of ATP by MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). The properties of the purified were the as for the The purified MukBEF was unstable and DNA dissociation of MukEF. MukEF and DNA bind MukB a This is at with as as the that MukBEF is a in MukB Rybenkov V.V. J. PubMed Scopus Google Scholar). The the function of MukEF were to displace MukB from DNA. A to in of two of association between MukB and MukEF. the was the binding of MukEF to was and could only at in the of is that MukBEF inside the cell in We the complex only at of MukEF Furthermore, the of purified was in DNA binding and that the MukBEF bind and DNA. that and are in E. in MukB MukBEF is to act as an In view kleisins and the SMC subunit of MukBEF are for different of chromosome DNA at the of the Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google is by the SMC of the complex. the DNA reshaping properties of the were virtually identical to those of MukB the complexes were in vitro or purified from the cell in the intracellular of condensins the of in The in the of MukB to the condensation of bacterial the of the The of kleisins is Kleisins are to bind only the of the V-shaped MukB distant SMCs kleisins an of chromatin that MukEF is to bridge of MukB. MukBEF was association between MukB and MukEF and Similarly, an that MukBEF in the of DNA K. M. K. K. S. Biochem. 2005; PubMed Scopus Google Scholar). the cell MukEF could act by directly distant or by MukB to as was of MukBEF Rybenkov V.V. J. PubMed Scopus Google Scholar) and the of of protein K. M. S. Mol. Microbiol. 2001; PubMed Scopus Google Scholar). In the of chromatin condensation by the interaction of kleisins with SMCs the chromosome the and the of kleisins or a of kleisins in the of chromatin The of of ATP in the of We not of ATP the of MukBEF not or the between DNA and MukEF ATP was to for DNA by MukB Z.M. Lai C.H. Rai R. Rybenkov V.V. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar) and the protein J.E. Crisona N.J. Belotserkovskii B.P. Lindsley J.E. Cozzarelli N.R. J. Biol. Chem. 2005; 280: 34723-34734Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar). These results are with the that ATP a of a rather the C.H. Schoffnegger D. Nishino T. Helmhart W. Nasmyth K. Lowe J. Mol. Cell. 2004; 15: 951-964Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar). MukB and the complex are stable in their in the of requires ATP for This with the that MukB is reaction The function of ATP is to promote dimerization of the head domains of SMCs (11Hopfner K.P. Karcher A. Shin D.S. Craig L. Arthur L.M. Carney J.P. Tainer J.A. Cell. 2000; 101: 789-800Abstract Full Text Full Text PDF PubMed Scopus (808) Google Scholar, 12Lammens A. Schele A. Hopfner K.P. Curr. Biol. 2004; 14: 1778-1782Abstract Full Text Full Text PDF PubMed Scopus (120) Google Scholar, 19Haering C.H. Schoffnegger D. Nishino T. Helmhart W. Nasmyth K. Lowe J. Mol. Cell. 2004; 15: 951-964Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar, 20Uhlmann F. Wernic D. Poupart M.A. Koonin E.V. Nasmyth K. Cell. 2000; 103: 375-386Abstract Full Text Full Text PDF PubMed Scopus (648) Google MukB not ATP for dimerization protein in the of kleisins from those by MukB MukBEF MukB at the of MukBEF disrupts The from to in in vitro is that ATP in The interaction between ATP and kleisins has been and A. Schele A. Hopfner K.P. Curr. Biol. 2004; 14: 1778-1782Abstract Full Text Full Text PDF PubMed Scopus (120) Google Scholar, 14Hirano M. Hirano T. EMBO J. 2004; 23: 2664-2673Crossref PubMed Scopus (103) Google Scholar, 19Haering C.H. Schoffnegger D. Nishino T. Helmhart W. Nasmyth K. Lowe J. Mol. Cell. 2004; 15: 951-964Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar). that kleisins displace DNA from MukB the functional to