Loading…

Identification and immunochemical location of UMP kinase from Bacillus subtilis

Phosphorylation of CMP and UMP is accomplished in Bacillus subtilis, as in Escherichia coli, by two different enzymes exhibiting characteristic structural and catalytic properties. UMP kinase from B. subtilis is an oligomer whose activity is strictly dependent on GTP. The B. subtilis enzyme is unsta...

Full description

Saved in:
Bibliographic Details
Published in:Current microbiology 2004-01, Vol.48 (1), p.62-67
Main Authors: Gagyi, Cristina, Ionescu, Mihaela, Gounon, Pierre, Sakamoto, Hiroshi, Rousselle, Jean-Claude, Laurent-Winter, Christine
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c355t-bca86c846937bb06f4ebd14eed74e0d8c335996d2d1fae04522134b372b202893
cites
container_end_page 67
container_issue 1
container_start_page 62
container_title Current microbiology
container_volume 48
creator Gagyi, Cristina
Ionescu, Mihaela
Gounon, Pierre
Sakamoto, Hiroshi
Rousselle, Jean-Claude
Laurent-Winter, Christine
description Phosphorylation of CMP and UMP is accomplished in Bacillus subtilis, as in Escherichia coli, by two different enzymes exhibiting characteristic structural and catalytic properties. UMP kinase from B. subtilis is an oligomer whose activity is strictly dependent on GTP. The B. subtilis enzyme is unstable in the absence of UTP, which acts as an allosteric inhibitor. Antibodies raised against recombinant B. subtilis UMP kinase recognized the protein both in soluble extract and in immunoelectron microscopy. UMP kinase from B. subtilis has a peripheral distribution which is related most probably to its role in the synthesis of membrane sugar components and its putative role in cell division.
doi_str_mv 10.1007/s00284-003-4117-2
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71726628</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17934889</sourcerecordid><originalsourceid>FETCH-LOGICAL-c355t-bca86c846937bb06f4ebd14eed74e0d8c335996d2d1fae04522134b372b202893</originalsourceid><addsrcrecordid>eNqFkT1PwzAQhi0EoqXwA1hQxMAWuLOd2B6h4ksqKgOdLcdxhEsSlzgZ-PektBISC9NJd8_7SqeHkHOEawQQNxGASp4CsJQjipQekClyRlNQCg_JFBhnqcwznJCTGNcASBXgMZlgBigRsilZPpeu7X3lrel9aBPTlolvmqEN9t0147ZO6rC_hSpZvbwmH7410SVVF5rkzlhf10NM4lD0vvbxlBxVpo7ubD9nZPVw_zZ_ShfLx-f57SK1LMv6tLBG5lbyXDFRFJBX3BUlcudKwR2U0jKWKZWXtMTKOOAZpch4wQQt6PizYjNytevddOFzcLHXjY_W1bVpXRiiFihonlP5L4hCMS5_Gi__gOswdO34hBZKKM6YzEYId5DtQoydq_Sm843pvjSC3jrROyd6dKK3TjQdMxf74qFoXPmb2Etg35oQhgY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>797943385</pqid></control><display><type>article</type><title>Identification and immunochemical location of UMP kinase from Bacillus subtilis</title><source>Springer Nature</source><creator>Gagyi, Cristina ; Ionescu, Mihaela ; Gounon, Pierre ; Sakamoto, Hiroshi ; Rousselle, Jean-Claude ; Laurent-Winter, Christine</creator><creatorcontrib>Gagyi, Cristina ; Ionescu, Mihaela ; Gounon, Pierre ; Sakamoto, Hiroshi ; Rousselle, Jean-Claude ; Laurent-Winter, Christine</creatorcontrib><description>Phosphorylation of CMP and UMP is accomplished in Bacillus subtilis, as in Escherichia coli, by two different enzymes exhibiting characteristic structural and catalytic properties. UMP kinase from B. subtilis is an oligomer whose activity is strictly dependent on GTP. The B. subtilis enzyme is unstable in the absence of UTP, which acts as an allosteric inhibitor. Antibodies raised against recombinant B. subtilis UMP kinase recognized the protein both in soluble extract and in immunoelectron microscopy. UMP kinase from B. subtilis has a peripheral distribution which is related most probably to its role in the synthesis of membrane sugar components and its putative role in cell division.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/s00284-003-4117-2</identifier><identifier>PMID: 15018105</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Bacillus subtilis ; Bacillus subtilis - enzymology ; Bacillus subtilis - ultrastructure ; Bacteria ; Bacterial Proteins - isolation &amp; purification ; Bacterial Proteins - metabolism ; Bacteriology ; Blotting, Western ; DNA, Bacterial - chemistry ; DNA, Bacterial - genetics ; E coli ; Electrophoresis, Gel, Two-Dimensional ; Guanosine Triphosphate - metabolism ; Immunohistochemistry ; Microscopy, Immunoelectron ; Nucleoside-Phosphate Kinase - isolation &amp; purification ; Nucleoside-Phosphate Kinase - metabolism ; Polymerase Chain Reaction</subject><ispartof>Current microbiology, 2004-01, Vol.48 (1), p.62-67</ispartof><rights>Springer-Verlag New York Inc. 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c355t-bca86c846937bb06f4ebd14eed74e0d8c335996d2d1fae04522134b372b202893</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15018105$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gagyi, Cristina</creatorcontrib><creatorcontrib>Ionescu, Mihaela</creatorcontrib><creatorcontrib>Gounon, Pierre</creatorcontrib><creatorcontrib>Sakamoto, Hiroshi</creatorcontrib><creatorcontrib>Rousselle, Jean-Claude</creatorcontrib><creatorcontrib>Laurent-Winter, Christine</creatorcontrib><title>Identification and immunochemical location of UMP kinase from Bacillus subtilis</title><title>Current microbiology</title><addtitle>Curr Microbiol</addtitle><description>Phosphorylation of CMP and UMP is accomplished in Bacillus subtilis, as in Escherichia coli, by two different enzymes exhibiting characteristic structural and catalytic properties. UMP kinase from B. subtilis is an oligomer whose activity is strictly dependent on GTP. The B. subtilis enzyme is unstable in the absence of UTP, which acts as an allosteric inhibitor. Antibodies raised against recombinant B. subtilis UMP kinase recognized the protein both in soluble extract and in immunoelectron microscopy. UMP kinase from B. subtilis has a peripheral distribution which is related most probably to its role in the synthesis of membrane sugar components and its putative role in cell division.</description><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - enzymology</subject><subject>Bacillus subtilis - ultrastructure</subject><subject>Bacteria</subject><subject>Bacterial Proteins - isolation &amp; purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Blotting, Western</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - genetics</subject><subject>E coli</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Immunohistochemistry</subject><subject>Microscopy, Immunoelectron</subject><subject>Nucleoside-Phosphate Kinase - isolation &amp; purification</subject><subject>Nucleoside-Phosphate Kinase - metabolism</subject><subject>Polymerase Chain Reaction</subject><issn>0343-8651</issn><issn>1432-0991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqFkT1PwzAQhi0EoqXwA1hQxMAWuLOd2B6h4ksqKgOdLcdxhEsSlzgZ-PektBISC9NJd8_7SqeHkHOEawQQNxGASp4CsJQjipQekClyRlNQCg_JFBhnqcwznJCTGNcASBXgMZlgBigRsilZPpeu7X3lrel9aBPTlolvmqEN9t0147ZO6rC_hSpZvbwmH7410SVVF5rkzlhf10NM4lD0vvbxlBxVpo7ubD9nZPVw_zZ_ShfLx-f57SK1LMv6tLBG5lbyXDFRFJBX3BUlcudKwR2U0jKWKZWXtMTKOOAZpch4wQQt6PizYjNytevddOFzcLHXjY_W1bVpXRiiFihonlP5L4hCMS5_Gi__gOswdO34hBZKKM6YzEYId5DtQoydq_Sm843pvjSC3jrROyd6dKK3TjQdMxf74qFoXPmb2Etg35oQhgY</recordid><startdate>200401</startdate><enddate>200401</enddate><creator>Gagyi, Cristina</creator><creator>Ionescu, Mihaela</creator><creator>Gounon, Pierre</creator><creator>Sakamoto, Hiroshi</creator><creator>Rousselle, Jean-Claude</creator><creator>Laurent-Winter, Christine</creator><general>Springer Nature B.V</general><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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200401</creationdate><title>Identification and immunochemical location of UMP kinase from Bacillus subtilis</title><author>Gagyi, Cristina ; Ionescu, Mihaela ; Gounon, Pierre ; Sakamoto, Hiroshi ; Rousselle, Jean-Claude ; Laurent-Winter, Christine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-bca86c846937bb06f4ebd14eed74e0d8c335996d2d1fae04522134b372b202893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - enzymology</topic><topic>Bacillus subtilis - ultrastructure</topic><topic>Bacteria</topic><topic>Bacterial Proteins - isolation &amp; purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Blotting, Western</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - genetics</topic><topic>E coli</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Immunohistochemistry</topic><topic>Microscopy, Immunoelectron</topic><topic>Nucleoside-Phosphate Kinase - isolation &amp; purification</topic><topic>Nucleoside-Phosphate Kinase - metabolism</topic><topic>Polymerase Chain Reaction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gagyi, Cristina</creatorcontrib><creatorcontrib>Ionescu, Mihaela</creatorcontrib><creatorcontrib>Gounon, Pierre</creatorcontrib><creatorcontrib>Sakamoto, Hiroshi</creatorcontrib><creatorcontrib>Rousselle, Jean-Claude</creatorcontrib><creatorcontrib>Laurent-Winter, Christine</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Current microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gagyi, Cristina</au><au>Ionescu, Mihaela</au><au>Gounon, Pierre</au><au>Sakamoto, Hiroshi</au><au>Rousselle, Jean-Claude</au><au>Laurent-Winter, Christine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and immunochemical location of UMP kinase from Bacillus subtilis</atitle><jtitle>Current microbiology</jtitle><addtitle>Curr Microbiol</addtitle><date>2004-01</date><risdate>2004</risdate><volume>48</volume><issue>1</issue><spage>62</spage><epage>67</epage><pages>62-67</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><abstract>Phosphorylation of CMP and UMP is accomplished in Bacillus subtilis, as in Escherichia coli, by two different enzymes exhibiting characteristic structural and catalytic properties. UMP kinase from B. subtilis is an oligomer whose activity is strictly dependent on GTP. The B. subtilis enzyme is unstable in the absence of UTP, which acts as an allosteric inhibitor. Antibodies raised against recombinant B. subtilis UMP kinase recognized the protein both in soluble extract and in immunoelectron microscopy. UMP kinase from B. subtilis has a peripheral distribution which is related most probably to its role in the synthesis of membrane sugar components and its putative role in cell division.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>15018105</pmid><doi>10.1007/s00284-003-4117-2</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0343-8651
ispartof Current microbiology, 2004-01, Vol.48 (1), p.62-67
issn 0343-8651
1432-0991
language eng
recordid cdi_proquest_miscellaneous_71726628
source Springer Nature
subjects Bacillus subtilis
Bacillus subtilis - enzymology
Bacillus subtilis - ultrastructure
Bacteria
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Bacteriology
Blotting, Western
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
E coli
Electrophoresis, Gel, Two-Dimensional
Guanosine Triphosphate - metabolism
Immunohistochemistry
Microscopy, Immunoelectron
Nucleoside-Phosphate Kinase - isolation & purification
Nucleoside-Phosphate Kinase - metabolism
Polymerase Chain Reaction
title Identification and immunochemical location of UMP kinase from Bacillus subtilis
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T00%3A20%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20and%20immunochemical%20location%20of%20UMP%20kinase%20from%20Bacillus%20subtilis&rft.jtitle=Current%20microbiology&rft.au=Gagyi,%20Cristina&rft.date=2004-01&rft.volume=48&rft.issue=1&rft.spage=62&rft.epage=67&rft.pages=62-67&rft.issn=0343-8651&rft.eissn=1432-0991&rft_id=info:doi/10.1007/s00284-003-4117-2&rft_dat=%3Cproquest_cross%3E17934889%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c355t-bca86c846937bb06f4ebd14eed74e0d8c335996d2d1fae04522134b372b202893%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=797943385&rft_id=info:pmid/15018105&rfr_iscdi=true