Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli
mukF , mukE and mukB genes are essential for the process of chromosome partitioning in Escherichia coli . We have studied protein–protein interactions among MukB, MukE and MukF proteins by co‐immunoprecipitation and sucrose gradient sedimentation experiments, using mukFEB null cells harboring plasmi...
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| Veröffentlicht in: | The EMBO journal 1999-11, Vol.18 (21), p.5873-5884 |
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| creator | Yamazoe, Mitsuyoshi Onogi, Toshinari Sunako, Yumi Niki, Hironori Yamanaka, Kunitoshi Ichimura, Toshiharu Hiraga, Sota |
| description | mukF
,
mukE
and
mukB
genes are essential for the process of chromosome partitioning in
Escherichia coli
. We have studied protein–protein interactions among MukB, MukE and MukF proteins by co‐immunoprecipitation and sucrose gradient sedimentation experiments, using
mukFEB
null cells harboring plasmids carrying the wild‐type or mutant‐type
mukFEB
operon. MukB forms a complex with MukF and MukE. Analysis of mutant MukB proteins suggested that MukF and MukE bind the C‐terminal globular domain of MukB. MukF is indispensable for an interaction between MukB and MukE; however, MukF itself is able to associate with MukB even in the absence of MukE. We have also found that MukF has a Ca
2+
‐binding activity. Although purified MukF was able to make a complex either with MukE or MukB, a complex consisting of the three Muk proteins was barely detected
in vitro
. However, increasing the Ca
2+
or Mg
2+
concentration in the reaction partially restored complex formation. This suggests that Ca
2+
or Mg
2+
may be required for the formation of a complex consisting of the three Muk proteins, and thus may participate in a particular step during chromosome partitioning. |
| doi_str_mv | 10.1093/emboj/18.21.5873 |
| format | Article |
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,
mukE
and
mukB
genes are essential for the process of chromosome partitioning in
Escherichia coli
. We have studied protein–protein interactions among MukB, MukE and MukF proteins by co‐immunoprecipitation and sucrose gradient sedimentation experiments, using
mukFEB
null cells harboring plasmids carrying the wild‐type or mutant‐type
mukFEB
operon. MukB forms a complex with MukF and MukE. Analysis of mutant MukB proteins suggested that MukF and MukE bind the C‐terminal globular domain of MukB. MukF is indispensable for an interaction between MukB and MukE; however, MukF itself is able to associate with MukB even in the absence of MukE. We have also found that MukF has a Ca
2+
‐binding activity. Although purified MukF was able to make a complex either with MukE or MukB, a complex consisting of the three Muk proteins was barely detected
in vitro
. However, increasing the Ca
2+
or Mg
2+
concentration in the reaction partially restored complex formation. This suggests that Ca
2+
or Mg
2+
may be required for the formation of a complex consisting of the three Muk proteins, and thus may participate in a particular step during chromosome partitioning.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/18.21.5873</identifier><identifier>PMID: 10545099</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Ca2+-binding protein ; Calcium - metabolism ; Centrifugation, Density Gradient ; Chromosomal Proteins, Non-Histone ; chromosome partitioning ; Chromosomes - genetics ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; E coli ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Genes, Bacterial ; Magnesium - metabolism ; Molecular Sequence Data ; motor protein ; mukB gene ; MukB protein ; MukB-MukE-MukF ; mukE gene ; MukE protein ; mukF gene ; MukF protein ; Mutation ; Precipitin Tests ; Protein Binding ; Proteins ; Repressor Proteins ; Sequence Alignment</subject><ispartof>The EMBO journal, 1999-11, Vol.18 (21), p.5873-5884</ispartof><rights>European Molecular Biology Organization 1999</rights><rights>Copyright © 1999 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Nov 01, 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6461-447db06bd03a94a6e08e31f3aa170b0b57ec4a5eb00f9165093f5a7327e0ae463</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171653/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171653/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10545099$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamazoe, Mitsuyoshi</creatorcontrib><creatorcontrib>Onogi, Toshinari</creatorcontrib><creatorcontrib>Sunako, Yumi</creatorcontrib><creatorcontrib>Niki, Hironori</creatorcontrib><creatorcontrib>Yamanaka, Kunitoshi</creatorcontrib><creatorcontrib>Ichimura, Toshiharu</creatorcontrib><creatorcontrib>Hiraga, Sota</creatorcontrib><title>Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>mukF
,
mukE
and
mukB
genes are essential for the process of chromosome partitioning in
Escherichia coli
. We have studied protein–protein interactions among MukB, MukE and MukF proteins by co‐immunoprecipitation and sucrose gradient sedimentation experiments, using
mukFEB
null cells harboring plasmids carrying the wild‐type or mutant‐type
mukFEB
operon. MukB forms a complex with MukF and MukE. Analysis of mutant MukB proteins suggested that MukF and MukE bind the C‐terminal globular domain of MukB. MukF is indispensable for an interaction between MukB and MukE; however, MukF itself is able to associate with MukB even in the absence of MukE. We have also found that MukF has a Ca
2+
‐binding activity. Although purified MukF was able to make a complex either with MukE or MukB, a complex consisting of the three Muk proteins was barely detected
in vitro
. However, increasing the Ca
2+
or Mg
2+
concentration in the reaction partially restored complex formation. This suggests that Ca
2+
or Mg
2+
may be required for the formation of a complex consisting of the three Muk proteins, and thus may participate in a particular step during chromosome partitioning.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Ca2+-binding protein</subject><subject>Calcium - metabolism</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromosomal Proteins, Non-Histone</subject><subject>chromosome partitioning</subject><subject>Chromosomes - genetics</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Genes, Bacterial</subject><subject>Magnesium - metabolism</subject><subject>Molecular Sequence Data</subject><subject>motor protein</subject><subject>mukB gene</subject><subject>MukB protein</subject><subject>MukB-MukE-MukF</subject><subject>mukE gene</subject><subject>MukE protein</subject><subject>mukF gene</subject><subject>MukF protein</subject><subject>Mutation</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Repressor Proteins</subject><subject>Sequence Alignment</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhSMEokvhzglFHDixW08c2_EFqV1tC2gLUgX0aDnJZNfbJA52srT_HodU1YKEerFHmu89z_hF0WsgCyCSnmCT290JZIsEFiwT9Ek0g5STeUIEexrNSMJhnkImj6IX3u8IIQGC59EREJYyIuUsMkvbdDXexpV1je6NbWNbxZfDzdn78VzFui3H4jzunO3RtD427d7WeyxDERdbZxvrbYNxp11vRgPTbsbWyhdbdKbYGh0XtjYvo2eVrj2-ur-Po-_nq2_Lj_P114tPy9P1vODpOG4qypzwvCRUy1RzJBlSqKjWIEhOciawSDXDnJBKAg9b0IppQROBRGPK6XH0YfLthrzBssC2d7pWnTONdnfKaqP-7rRmqzZ2rwBE8KPB4N29gbM_B_S9aowvsK51i3bwisskYYzBoyAIKjnLkgC-_Qfc2cG14RcUSBZCykgWIDJBhbPeO6weRgaixrTVn7QVZCoBNaYdJG8OVz0QTPEGQE7AL1Pj3aOGanV59lkwCVKO28Gk9UHWbtAdDP3_geaTxvgebx_e0-5GcUEFU9dfLtR1wtZX4gdXV_Q3KSvYzg</recordid><startdate>19991101</startdate><enddate>19991101</enddate><creator>Yamazoe, Mitsuyoshi</creator><creator>Onogi, Toshinari</creator><creator>Sunako, Yumi</creator><creator>Niki, Hironori</creator><creator>Yamanaka, Kunitoshi</creator><creator>Ichimura, Toshiharu</creator><creator>Hiraga, Sota</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19991101</creationdate><title>Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli</title><author>Yamazoe, Mitsuyoshi ; Onogi, Toshinari ; Sunako, Yumi ; Niki, Hironori ; Yamanaka, Kunitoshi ; Ichimura, Toshiharu ; Hiraga, Sota</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6461-447db06bd03a94a6e08e31f3aa170b0b57ec4a5eb00f9165093f5a7327e0ae463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Ca2+-binding protein</topic><topic>Calcium - metabolism</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromosomal Proteins, Non-Histone</topic><topic>chromosome partitioning</topic><topic>Chromosomes - genetics</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>Genes, Bacterial</topic><topic>Magnesium - metabolism</topic><topic>Molecular Sequence Data</topic><topic>motor protein</topic><topic>mukB gene</topic><topic>MukB protein</topic><topic>MukB-MukE-MukF</topic><topic>mukE gene</topic><topic>MukE protein</topic><topic>mukF gene</topic><topic>MukF protein</topic><topic>Mutation</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Repressor Proteins</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamazoe, Mitsuyoshi</creatorcontrib><creatorcontrib>Onogi, Toshinari</creatorcontrib><creatorcontrib>Sunako, Yumi</creatorcontrib><creatorcontrib>Niki, Hironori</creatorcontrib><creatorcontrib>Yamanaka, Kunitoshi</creatorcontrib><creatorcontrib>Ichimura, Toshiharu</creatorcontrib><creatorcontrib>Hiraga, Sota</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamazoe, Mitsuyoshi</au><au>Onogi, Toshinari</au><au>Sunako, Yumi</au><au>Niki, Hironori</au><au>Yamanaka, Kunitoshi</au><au>Ichimura, Toshiharu</au><au>Hiraga, Sota</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>1999-11-01</date><risdate>1999</risdate><volume>18</volume><issue>21</issue><spage>5873</spage><epage>5884</epage><pages>5873-5884</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>mukF
,
mukE
and
mukB
genes are essential for the process of chromosome partitioning in
Escherichia coli
. We have studied protein–protein interactions among MukB, MukE and MukF proteins by co‐immunoprecipitation and sucrose gradient sedimentation experiments, using
mukFEB
null cells harboring plasmids carrying the wild‐type or mutant‐type
mukFEB
operon. MukB forms a complex with MukF and MukE. Analysis of mutant MukB proteins suggested that MukF and MukE bind the C‐terminal globular domain of MukB. MukF is indispensable for an interaction between MukB and MukE; however, MukF itself is able to associate with MukB even in the absence of MukE. We have also found that MukF has a Ca
2+
‐binding activity. Although purified MukF was able to make a complex either with MukE or MukB, a complex consisting of the three Muk proteins was barely detected
in vitro
. However, increasing the Ca
2+
or Mg
2+
concentration in the reaction partially restored complex formation. This suggests that Ca
2+
or Mg
2+
may be required for the formation of a complex consisting of the three Muk proteins, and thus may participate in a particular step during chromosome partitioning.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>10545099</pmid><doi>10.1093/emboj/18.21.5873</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 1999-11, Vol.18 (21), p.5873-5884 |
| issn | 0261-4189 1460-2075 1460-2075 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1171653 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Bacterial Proteins - genetics Bacterial Proteins - metabolism Ca2+-binding protein Calcium - metabolism Centrifugation, Density Gradient Chromosomal Proteins, Non-Histone chromosome partitioning Chromosomes - genetics DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism E coli Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Genes, Bacterial Magnesium - metabolism Molecular Sequence Data motor protein mukB gene MukB protein MukB-MukE-MukF mukE gene MukE protein mukF gene MukF protein Mutation Precipitin Tests Protein Binding Proteins Repressor Proteins Sequence Alignment |
| title | Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli |
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