Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum
To characterize cytoskeletal components of archaea, the ftsZ gene from Thermoplasma acidophilum was cloned and sequenced. In T. acidophilum ftsZ, which is involved in cell division, was found to be in an operon with the pyrF gene, which encodes orotidine-5′-monophosphate decarboxylase (ODC), an esse...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2000-09, Vol.275 (3), p.936-945 |
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| creator | Yaoi, Takuro Laksanalamai, Pongpan Jiemjit, Anchalee Kagawa, Hiromi K. Alton, Thomas Trent, Jonathan D. |
| description | To characterize cytoskeletal components of archaea, the ftsZ gene from Thermoplasma acidophilum was cloned and sequenced. In T. acidophilum ftsZ, which is involved in cell division, was found to be in an operon with the pyrF gene, which encodes orotidine-5′-monophosphate decarboxylase (ODC), an essential enzyme in pyrimidine biosynthesis. Both ftsZ and pyrF from T. acidophilum were expressed in Escherichia coli and formed functional proteins. FtsZ expression in wild-type E. coli resulted in the filamentous phenotype characteristic of ftsZ mutants. T. acidophilum pyrF expression in an E. coli mutant lacking pyrF complemented the mutation and rescued the strain. Sequence alignments of ODCs from archaea, bacteria, and eukarya reveal five conserved regions, two of which have homology to 3-hexulose-6-phosphate synthase (HPS), suggesting a common substrate recognition and binding motif. |
| doi_str_mv | 10.1006/bbrc.2000.3401 |
| format | Article |
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In T. acidophilum ftsZ, which is involved in cell division, was found to be in an operon with the pyrF gene, which encodes orotidine-5′-monophosphate decarboxylase (ODC), an essential enzyme in pyrimidine biosynthesis. Both ftsZ and pyrF from T. acidophilum were expressed in Escherichia coli and formed functional proteins. FtsZ expression in wild-type E. coli resulted in the filamentous phenotype characteristic of ftsZ mutants. T. acidophilum pyrF expression in an E. coli mutant lacking pyrF complemented the mutation and rescued the strain. Sequence alignments of ODCs from archaea, bacteria, and eukarya reveal five conserved regions, two of which have homology to 3-hexulose-6-phosphate synthase (HPS), suggesting a common substrate recognition and binding motif.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2000.3401</identifier><identifier>PMID: 10973825</identifier><language>eng</language><publisher>Legacy CDMS: Elsevier Inc</publisher><subject>Amino Acid Sequence ; archaea ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Base Sequence ; Binding Sites ; Cell Division ; Cloning, Molecular ; Codon, Initiator - genetics ; Conserved Sequence - genetics ; Cytoskeletal Proteins ; cytoskeleton ; Escherichia coli ; Escherichia coli - genetics ; ftsZ gene ; Genetic Complementation Test ; genetics ; Life Sciences (General) ; molecular evolution ; Molecular Sequence Data ; Mutation ; Operon - genetics ; orotidine 5'-monophosphate decarboxylase ; Orotidine-5'-Phosphate Decarboxylase - chemistry ; Orotidine-5'-Phosphate Decarboxylase - genetics ; Orotidine-5'-Phosphate Decarboxylase - metabolism ; Phenotype ; Promoter Regions, Genetic - genetics ; pyrF gene ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Restriction Mapping ; Sequence Alignment ; Space life sciences ; Thermoplasma - enzymology ; Thermoplasma - genetics ; Thermoplasma acidophilum</subject><ispartof>Biochemical and biophysical research communications, 2000-09, Vol.275 (3), p.936-945</ispartof><rights>2000 Academic Press</rights><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-afa2f84bd27b425cea3a356a44ad6dc01095555197222ea6d0125abaa33d440f3</citedby><cites>FETCH-LOGICAL-c392t-afa2f84bd27b425cea3a356a44ad6dc01095555197222ea6d0125abaa33d440f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2000.3401$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10973825$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yaoi, Takuro</creatorcontrib><creatorcontrib>Laksanalamai, Pongpan</creatorcontrib><creatorcontrib>Jiemjit, Anchalee</creatorcontrib><creatorcontrib>Kagawa, Hiromi K.</creatorcontrib><creatorcontrib>Alton, Thomas</creatorcontrib><creatorcontrib>Trent, Jonathan D.</creatorcontrib><title>Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>To characterize cytoskeletal components of archaea, the ftsZ gene from Thermoplasma acidophilum was cloned and sequenced. In T. acidophilum ftsZ, which is involved in cell division, was found to be in an operon with the pyrF gene, which encodes orotidine-5′-monophosphate decarboxylase (ODC), an essential enzyme in pyrimidine biosynthesis. Both ftsZ and pyrF from T. acidophilum were expressed in Escherichia coli and formed functional proteins. FtsZ expression in wild-type E. coli resulted in the filamentous phenotype characteristic of ftsZ mutants. T. acidophilum pyrF expression in an E. coli mutant lacking pyrF complemented the mutation and rescued the strain. Sequence alignments of ODCs from archaea, bacteria, and eukarya reveal five conserved regions, two of which have homology to 3-hexulose-6-phosphate synthase (HPS), suggesting a common substrate recognition and binding motif.</description><subject>Amino Acid Sequence</subject><subject>archaea</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Cell Division</subject><subject>Cloning, Molecular</subject><subject>Codon, Initiator - genetics</subject><subject>Conserved Sequence - genetics</subject><subject>Cytoskeletal Proteins</subject><subject>cytoskeleton</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>ftsZ gene</subject><subject>Genetic Complementation Test</subject><subject>genetics</subject><subject>Life Sciences (General)</subject><subject>molecular evolution</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Operon - genetics</subject><subject>orotidine 5'-monophosphate decarboxylase</subject><subject>Orotidine-5'-Phosphate Decarboxylase - chemistry</subject><subject>Orotidine-5'-Phosphate Decarboxylase - genetics</subject><subject>Orotidine-5'-Phosphate Decarboxylase - metabolism</subject><subject>Phenotype</subject><subject>Promoter Regions, Genetic - genetics</subject><subject>pyrF gene</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Restriction Mapping</subject><subject>Sequence Alignment</subject><subject>Space life sciences</subject><subject>Thermoplasma - enzymology</subject><subject>Thermoplasma - genetics</subject><subject>Thermoplasma acidophilum</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><recordid>eNqFkEtP3DAURi0Egum0264QyopdBr_yWqIRQyshdTNIiI11Y980Rkkc7Eyl6a_HISzYVLUXlvyd79o6hHxndMMozW_q2usNp5RuhKTshKwYrWjKGZWnZBWv85RX7OmCfAnhhVLGZF6dk4sIFaLk2Yo8bTs32OF3AoNJti140BN6-xcm64bENUkzhef3cDz6XdJ41ydTi8mt1y1gRPYt-t6NHYQeEtDWuLG13aH_Ss4a6AJ--zjX5HF3t9_-SB9-3f_c3j6kWlR8SqEB3pSyNryoJc80ggCR5SAlmNxoGn-axcWqgnOOkBvKeAY1gBBGStqINble5o7evR4wTKq3QWPXwYDuEFTsibIU_L8gK_KorcgjuFlA7V0IHhs1etuDPypG1SxdzdLVLF3N0mPh6mPyoe7RfMIXyxG4XIABAqhh8mFux6qMW8S4XGKMnv5Y9Cpoi4NGYz3qSRln__X0G0JCmLg</recordid><startdate>20000907</startdate><enddate>20000907</enddate><creator>Yaoi, Takuro</creator><creator>Laksanalamai, Pongpan</creator><creator>Jiemjit, Anchalee</creator><creator>Kagawa, Hiromi K.</creator><creator>Alton, Thomas</creator><creator>Trent, Jonathan D.</creator><general>Elsevier Inc</general><scope>CYE</scope><scope>CYI</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000907</creationdate><title>Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum</title><author>Yaoi, Takuro ; Laksanalamai, Pongpan ; Jiemjit, Anchalee ; Kagawa, Hiromi K. ; Alton, Thomas ; Trent, Jonathan D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-afa2f84bd27b425cea3a356a44ad6dc01095555197222ea6d0125abaa33d440f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>archaea</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Cell Division</topic><topic>Cloning, Molecular</topic><topic>Codon, Initiator - genetics</topic><topic>Conserved Sequence - genetics</topic><topic>Cytoskeletal Proteins</topic><topic>cytoskeleton</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>ftsZ gene</topic><topic>Genetic Complementation Test</topic><topic>genetics</topic><topic>Life Sciences (General)</topic><topic>molecular evolution</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Operon - genetics</topic><topic>orotidine 5'-monophosphate decarboxylase</topic><topic>Orotidine-5'-Phosphate Decarboxylase - chemistry</topic><topic>Orotidine-5'-Phosphate Decarboxylase - genetics</topic><topic>Orotidine-5'-Phosphate Decarboxylase - metabolism</topic><topic>Phenotype</topic><topic>Promoter Regions, Genetic - genetics</topic><topic>pyrF gene</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Restriction Mapping</topic><topic>Sequence Alignment</topic><topic>Space life sciences</topic><topic>Thermoplasma - enzymology</topic><topic>Thermoplasma - genetics</topic><topic>Thermoplasma acidophilum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yaoi, Takuro</creatorcontrib><creatorcontrib>Laksanalamai, Pongpan</creatorcontrib><creatorcontrib>Jiemjit, Anchalee</creatorcontrib><creatorcontrib>Kagawa, Hiromi K.</creatorcontrib><creatorcontrib>Alton, Thomas</creatorcontrib><creatorcontrib>Trent, Jonathan D.</creatorcontrib><collection>NASA Scientific and Technical Information</collection><collection>NASA Technical Reports Server</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yaoi, Takuro</au><au>Laksanalamai, Pongpan</au><au>Jiemjit, Anchalee</au><au>Kagawa, Hiromi K.</au><au>Alton, Thomas</au><au>Trent, Jonathan D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2000-09-07</date><risdate>2000</risdate><volume>275</volume><issue>3</issue><spage>936</spage><epage>945</epage><pages>936-945</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>To characterize cytoskeletal components of archaea, the ftsZ gene from Thermoplasma acidophilum was cloned and sequenced. In T. acidophilum ftsZ, which is involved in cell division, was found to be in an operon with the pyrF gene, which encodes orotidine-5′-monophosphate decarboxylase (ODC), an essential enzyme in pyrimidine biosynthesis. Both ftsZ and pyrF from T. acidophilum were expressed in Escherichia coli and formed functional proteins. FtsZ expression in wild-type E. coli resulted in the filamentous phenotype characteristic of ftsZ mutants. T. acidophilum pyrF expression in an E. coli mutant lacking pyrF complemented the mutation and rescued the strain. Sequence alignments of ODCs from archaea, bacteria, and eukarya reveal five conserved regions, two of which have homology to 3-hexulose-6-phosphate synthase (HPS), suggesting a common substrate recognition and binding motif.</abstract><cop>Legacy CDMS</cop><pub>Elsevier Inc</pub><pmid>10973825</pmid><doi>10.1006/bbrc.2000.3401</doi><tpages>10</tpages></addata></record> |
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| subjects | Amino Acid Sequence archaea Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Binding Sites Cell Division Cloning, Molecular Codon, Initiator - genetics Conserved Sequence - genetics Cytoskeletal Proteins cytoskeleton Escherichia coli Escherichia coli - genetics ftsZ gene Genetic Complementation Test genetics Life Sciences (General) molecular evolution Molecular Sequence Data Mutation Operon - genetics orotidine 5'-monophosphate decarboxylase Orotidine-5'-Phosphate Decarboxylase - chemistry Orotidine-5'-Phosphate Decarboxylase - genetics Orotidine-5'-Phosphate Decarboxylase - metabolism Phenotype Promoter Regions, Genetic - genetics pyrF gene Recombinant Proteins - chemistry Recombinant Proteins - metabolism Restriction Mapping Sequence Alignment Space life sciences Thermoplasma - enzymology Thermoplasma - genetics Thermoplasma acidophilum |
| title | Cloning and Characterization of ftsZ and pyrF from the Archaeon Thermoplasma acidophilum |
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