Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869
A 20-kDa Brevibacterium lactofermentum protein was detected when purifying the His-tagged FtsZ BL. The protein was identified by matrix-assisted laser desorption/ionisation time of flight as the inorganic pyrophosphatase encoded by the ppa gene, which is present as a single copy in the genome of Cor...
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| Veröffentlicht in: | FEMS microbiology letters 2003-08, Vol.225 (1), p.85-92 |
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| creator | Ramos, Angelina Adham, Sirin A.I. Gil, José A. |
| description | A 20-kDa
Brevibacterium lactofermentum protein was detected when purifying the His-tagged FtsZ
BL. The protein was identified by matrix-assisted laser desorption/ionisation time of flight as the inorganic pyrophosphatase encoded by the
ppa gene, which is present as a single copy in the genome of
Corynebacterium glutamicum. The
ppa gene was cloned from
B. lactofermentum chromosomal DNA by polymerase chain reaction; it seemed to be an essential gene and it might represent an attractive target for drug discovery. The cloned
ppa gene complemented a
ppa−
Escherichia coli mutant and a
ppa-gfp gene fusion revealed that the gene product mainly accumulated at the cell poles in both
E. coli and
B. lactofermentum. |
| doi_str_mv | 10.1016/S0378-1097(03)00485-3 |
| format | Article |
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Brevibacterium lactofermentum protein was detected when purifying the His-tagged FtsZ
BL. The protein was identified by matrix-assisted laser desorption/ionisation time of flight as the inorganic pyrophosphatase encoded by the
ppa gene, which is present as a single copy in the genome of
Corynebacterium glutamicum. The
ppa gene was cloned from
B. lactofermentum chromosomal DNA by polymerase chain reaction; it seemed to be an essential gene and it might represent an attractive target for drug discovery. The cloned
ppa gene complemented a
ppa−
Escherichia coli mutant and a
ppa-gfp gene fusion revealed that the gene product mainly accumulated at the cell poles in both
E. coli and
B. lactofermentum.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/S0378-1097(03)00485-3</identifier><identifier>PMID: 12900025</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Elsevier B.V</publisher><subject>Bacteriology ; Base Sequence ; Biological and medical sciences ; Brevibacterium - enzymology ; Brevibacterium - genetics ; Cell division ; Cloning, Molecular ; Corynebacterium ; Corynebacterium - enzymology ; Corynebacterium - genetics ; DivIVA ; Escherichia coli - enzymology ; Escherichia coli - genetics ; FtsZ ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Genes, Bacterial ; Genetic Complementation Test ; Genetics ; Green fluorescence protein ; Green Fluorescent Proteins ; Inorganic pyrophosphatase ; Inorganic Pyrophosphatase - genetics ; Inorganic Pyrophosphatase - metabolism ; Luminescent Proteins - genetics ; Luminescent Proteins - metabolism ; Microbiology ; Plasmids - genetics ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Subcellular Fractions - enzymology</subject><ispartof>FEMS microbiology letters, 2003-08, Vol.225 (1), p.85-92</ispartof><rights>2003 Federation of European Microbiological Societies</rights><rights>2003 Federation of European Microbiological Societies 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5125-fcf60ff09797f29a76ce1b0a171dff7e44f48f9ad2113f105133c43a3592b0d53</citedby><cites>FETCH-LOGICAL-c5125-fcf60ff09797f29a76ce1b0a171dff7e44f48f9ad2113f105133c43a3592b0d53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0378-1097%2803%2900485-3$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2FS0378-1097%2803%2900485-3$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15204019$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12900025$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ramos, Angelina</creatorcontrib><creatorcontrib>Adham, Sirin A.I.</creatorcontrib><creatorcontrib>Gil, José A.</creatorcontrib><title>Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>A 20-kDa
Brevibacterium lactofermentum protein was detected when purifying the His-tagged FtsZ
BL. The protein was identified by matrix-assisted laser desorption/ionisation time of flight as the inorganic pyrophosphatase encoded by the
ppa gene, which is present as a single copy in the genome of
Corynebacterium glutamicum. The
ppa gene was cloned from
B. lactofermentum chromosomal DNA by polymerase chain reaction; it seemed to be an essential gene and it might represent an attractive target for drug discovery. The cloned
ppa gene complemented a
ppa−
Escherichia coli mutant and a
ppa-gfp gene fusion revealed that the gene product mainly accumulated at the cell poles in both
E. coli and
B. lactofermentum.</description><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Brevibacterium - enzymology</subject><subject>Brevibacterium - genetics</subject><subject>Cell division</subject><subject>Cloning, Molecular</subject><subject>Corynebacterium</subject><subject>Corynebacterium - enzymology</subject><subject>Corynebacterium - genetics</subject><subject>DivIVA</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>FtsZ</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Genes, Bacterial</subject><subject>Genetic Complementation Test</subject><subject>Genetics</subject><subject>Green fluorescence protein</subject><subject>Green Fluorescent Proteins</subject><subject>Inorganic pyrophosphatase</subject><subject>Inorganic Pyrophosphatase - genetics</subject><subject>Inorganic Pyrophosphatase - metabolism</subject><subject>Luminescent Proteins - genetics</subject><subject>Luminescent Proteins - metabolism</subject><subject>Microbiology</subject><subject>Plasmids - genetics</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Subcellular Fractions - enzymology</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkVGL1DAUhYMo7rj6E5S8KPpQTZomTZ-WtbgqjPjg-hwy6c1MpE1q0q7Oq7_cdGZwEYT1KffCd3LO5SD0lJLXlFDx5gthtSwoaeqXhL0ipJK8YPfQivK6KkQj5H20-oOcoUcpfSOZKol4iM5o2eSl5Cv0q-2Dd36Lte8w_BwjpOSCx8HiaQfY-RC32juDx30M4y6kcacnnQBvwQO2MQwHTg-ZxNq4Do8xdLOBiN9GuHEbbSaIbh5wn6dgIQ7gp7xeXrctpkyK5jF6YHWf4MnpPUdfr95dtx-K9ef3H9vLdWE4LXlhjRXE2nxNU9uy0bUwQDdE05p21tZQVbaSttFdSSmzlHDKmKmYZrwpN6Tj7By9OP6bE36fIU1qcMlA32sPYU6qZpwJUok7QSqlKKVsMsiPoIkhpQhWjdENOu4VJWppSR1aUksFijB1aEmxrHt2Mpg3A3S3qlMtGXh-AnQyurdRe-PSLcdLUhG6BJBH7ofrYf9_7urq01ouFuQoDfP4b2Hxl7BYYl8cJZBbunEQVTIOvIHORTCT6oK74_Df0QrNbA</recordid><startdate>20030808</startdate><enddate>20030808</enddate><creator>Ramos, Angelina</creator><creator>Adham, Sirin A.I.</creator><creator>Gil, José A.</creator><general>Elsevier B.V</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20030808</creationdate><title>Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869</title><author>Ramos, Angelina ; Adham, Sirin A.I. ; Gil, José A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5125-fcf60ff09797f29a76ce1b0a171dff7e44f48f9ad2113f105133c43a3592b0d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Brevibacterium - enzymology</topic><topic>Brevibacterium - genetics</topic><topic>Cell division</topic><topic>Cloning, Molecular</topic><topic>Corynebacterium</topic><topic>Corynebacterium - enzymology</topic><topic>Corynebacterium - genetics</topic><topic>DivIVA</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>FtsZ</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Genes, Bacterial</topic><topic>Genetic Complementation Test</topic><topic>Genetics</topic><topic>Green fluorescence protein</topic><topic>Green Fluorescent Proteins</topic><topic>Inorganic pyrophosphatase</topic><topic>Inorganic Pyrophosphatase - genetics</topic><topic>Inorganic Pyrophosphatase - metabolism</topic><topic>Luminescent Proteins - genetics</topic><topic>Luminescent Proteins - metabolism</topic><topic>Microbiology</topic><topic>Plasmids - genetics</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Subcellular Fractions - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ramos, Angelina</creatorcontrib><creatorcontrib>Adham, Sirin A.I.</creatorcontrib><creatorcontrib>Gil, José A.</creatorcontrib><collection>Pascal-Francis</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>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>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ramos, Angelina</au><au>Adham, Sirin A.I.</au><au>Gil, José A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2003-08-08</date><risdate>2003</risdate><volume>225</volume><issue>1</issue><spage>85</spage><epage>92</epage><pages>85-92</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>A 20-kDa
Brevibacterium lactofermentum protein was detected when purifying the His-tagged FtsZ
BL. The protein was identified by matrix-assisted laser desorption/ionisation time of flight as the inorganic pyrophosphatase encoded by the
ppa gene, which is present as a single copy in the genome of
Corynebacterium glutamicum. The
ppa gene was cloned from
B. lactofermentum chromosomal DNA by polymerase chain reaction; it seemed to be an essential gene and it might represent an attractive target for drug discovery. The cloned
ppa gene complemented a
ppa−
Escherichia coli mutant and a
ppa-gfp gene fusion revealed that the gene product mainly accumulated at the cell poles in both
E. coli and
B. lactofermentum.</abstract><cop>Oxford, UK</cop><pub>Elsevier B.V</pub><pmid>12900025</pmid><doi>10.1016/S0378-1097(03)00485-3</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | FEMS microbiology letters, 2003-08, Vol.225 (1), p.85-92 |
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| source | MEDLINE; Wiley Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Bacteriology Base Sequence Biological and medical sciences Brevibacterium - enzymology Brevibacterium - genetics Cell division Cloning, Molecular Corynebacterium Corynebacterium - enzymology Corynebacterium - genetics DivIVA Escherichia coli - enzymology Escherichia coli - genetics FtsZ Fundamental and applied biological sciences. Psychology Gene Expression Genes, Bacterial Genetic Complementation Test Genetics Green fluorescence protein Green Fluorescent Proteins Inorganic pyrophosphatase Inorganic Pyrophosphatase - genetics Inorganic Pyrophosphatase - metabolism Luminescent Proteins - genetics Luminescent Proteins - metabolism Microbiology Plasmids - genetics Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Subcellular Fractions - enzymology |
| title | Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869 |
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