In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa
Abstract Bacterial peptidoglycan is the cell wall component responsible for maintaining cell integrity against osmotic pressure. Biosynthesis of the cytoplasmic precursor UDP-N-acetylmuramyl pentapeptide is catalyzed by the Mur enzymes. Genomic analysis of the three regions encoding Mur proteins was...
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| Veröffentlicht in: | FEMS microbiology letters 2001-07, Vol.201 (2), p.229-235 |
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| creator | El Zoeiby, Ahmed Sanschagrin, François Havugimana, Pierre C. Garnier, Alain Levesque, Roger C. |
| description | Abstract
Bacterial peptidoglycan is the cell wall component responsible for maintaining cell integrity against osmotic pressure. Biosynthesis of the cytoplasmic precursor UDP-N-acetylmuramyl pentapeptide is catalyzed by the Mur enzymes. Genomic analysis of the three regions encoding Mur proteins was achieved. We have cloned and over-expressed the murA, -B, -D, -E and -F genes of Pseudomonas aeruginosa in pET expression system by adding a His–Tag to the C-termini of the proteins. Mur proteins were purified to homogeneity by a single chromatographic step on affinity nickel columns. Protein identities were verified through N-terminal sequencing. Enzyme activity was proved by the identification of the pathway's final product. |
| doi_str_mv | 10.1111/j.1574-6968.2001.tb10761.x |
| format | Article |
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Bacterial peptidoglycan is the cell wall component responsible for maintaining cell integrity against osmotic pressure. Biosynthesis of the cytoplasmic precursor UDP-N-acetylmuramyl pentapeptide is catalyzed by the Mur enzymes. Genomic analysis of the three regions encoding Mur proteins was achieved. We have cloned and over-expressed the murA, -B, -D, -E and -F genes of Pseudomonas aeruginosa in pET expression system by adding a His–Tag to the C-termini of the proteins. Mur proteins were purified to homogeneity by a single chromatographic step on affinity nickel columns. Protein identities were verified through N-terminal sequencing. Enzyme activity was proved by the identification of the pathway's final product.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2001.tb10761.x</identifier><identifier>PMID: 11470366</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Bacterial cell wall ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Biosynthesis ; Cell Wall - metabolism ; Cell wall biosynthesis gene ; Cell walls ; Chromatography, Affinity ; Cloning, Molecular ; Enzymatic activity ; Enzyme activity ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Genes, Bacterial - genetics ; Genomic analysis ; Microbiology ; Molecular Sequence Data ; Motility, taxis ; Mur enzyme ; MurA protein ; MurB protein ; MurD protein ; MurE protein ; MurF protein ; Nickel ; Osmosis ; Osmotic pressure ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Peptidoglycan ; Peptidoglycan - biosynthesis ; Peptidoglycan - genetics ; Peptidoglycans ; Precursors ; Proteins ; Pseudomonas aeruginosa ; Pseudomonas aeruginosa - enzymology ; Pseudomonas aeruginosa - genetics ; Pseudomonas aeruginosa - growth & development ; Pseudomonas aeruginosa - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Sequence Analysis, DNA ; Sequence Analysis, Protein</subject><ispartof>FEMS microbiology letters, 2001-07, Vol.201 (2), p.229-235</ispartof><rights>2001 Federation of European Microbiological Societies 2001</rights><rights>2002 INIST-CNRS</rights><rights>2001 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4049-6059f4a461c8ba5eac92b17cee11d85d13a5d083c51067486ac90e4799f36b913</citedby><cites>FETCH-LOGICAL-c4049-6059f4a461c8ba5eac92b17cee11d85d13a5d083c51067486ac90e4799f36b913</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2001.tb10761.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2001.tb10761.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14161265$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11470366$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>El Zoeiby, Ahmed</creatorcontrib><creatorcontrib>Sanschagrin, François</creatorcontrib><creatorcontrib>Havugimana, Pierre C.</creatorcontrib><creatorcontrib>Garnier, Alain</creatorcontrib><creatorcontrib>Levesque, Roger C.</creatorcontrib><title>In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Bacterial peptidoglycan is the cell wall component responsible for maintaining cell integrity against osmotic pressure. Biosynthesis of the cytoplasmic precursor UDP-N-acetylmuramyl pentapeptide is catalyzed by the Mur enzymes. Genomic analysis of the three regions encoding Mur proteins was achieved. We have cloned and over-expressed the murA, -B, -D, -E and -F genes of Pseudomonas aeruginosa in pET expression system by adding a His–Tag to the C-termini of the proteins. Mur proteins were purified to homogeneity by a single chromatographic step on affinity nickel columns. Protein identities were verified through N-terminal sequencing. Enzyme activity was proved by the identification of the pathway's final product.</description><subject>Amino Acid Sequence</subject><subject>Bacterial cell wall</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biosynthesis</subject><subject>Cell Wall - metabolism</subject><subject>Cell wall biosynthesis gene</subject><subject>Cell walls</subject><subject>Chromatography, Affinity</subject><subject>Cloning, Molecular</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genes, Bacterial - genetics</subject><subject>Genomic analysis</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Motility, taxis</subject><subject>Mur enzyme</subject><subject>MurA protein</subject><subject>MurB protein</subject><subject>MurD protein</subject><subject>MurE protein</subject><subject>MurF protein</subject><subject>Nickel</subject><subject>Osmosis</subject><subject>Osmotic pressure</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Peptidoglycan</subject><subject>Peptidoglycan - biosynthesis</subject><subject>Peptidoglycan - genetics</subject><subject>Peptidoglycans</subject><subject>Precursors</subject><subject>Proteins</subject><subject>Pseudomonas aeruginosa</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Pseudomonas aeruginosa - genetics</subject><subject>Pseudomonas aeruginosa - growth & development</subject><subject>Pseudomonas aeruginosa - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Analysis, Protein</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqVkdFr1TAUxoso7m76L0hQ3FvrOW2Stj4MZDgdXNEHfQ5pmm65tElNUrf-97bc4kAUMS8JnN_3nXx8SfISIcPlvDlkyEqa8ppXWQ6AWWwQSo7Z_aNk92v0ONlBUVYpQl2eJKchHACA5sCfJieItISC810Sry35YaJ3xGvlbIh-UtE4S1xH4q0mjXFhtssrGkVGGW_v5LzORj1G07qbflbSEjVHN_YyDCu0GE0-OE-MJV-Cnlo3OCsDkdpPN8a6IJ8lTzrZB_18u8-Sb1fvv15-TPefP1xfvtunigKtUw6s7qikHFXVSKalqvMGS6U1YluxFgvJWqgKxRB4SSu-AKBpWdddwZsai7Pk_Og7evd90iGKwQSl-15a7aYgSoQCcw7_BLGCCnKsF_DVb-DBTd4uIUReIALjOVv3vj1SyrsQvO7E6M0g_SwQxFqhOIi1J7H2JNYKxVahuF_EL7YVUzPo9kG6dbYArzdABiX7zkurTHjgKPIlFFu4iyN3Z3o9_8cXxNWnfZ6vYdnRwE3jX-TpnxL8BCwEyfE</recordid><startdate>200107</startdate><enddate>200107</enddate><creator>El Zoeiby, Ahmed</creator><creator>Sanschagrin, François</creator><creator>Havugimana, Pierre C.</creator><creator>Garnier, Alain</creator><creator>Levesque, Roger C.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200107</creationdate><title>In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa</title><author>El Zoeiby, Ahmed ; Sanschagrin, François ; Havugimana, Pierre C. ; Garnier, Alain ; Levesque, Roger C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4049-6059f4a461c8ba5eac92b17cee11d85d13a5d083c51067486ac90e4799f36b913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial cell wall</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biosynthesis</topic><topic>Cell Wall - metabolism</topic><topic>Cell wall biosynthesis gene</topic><topic>Cell walls</topic><topic>Chromatography, Affinity</topic><topic>Cloning, Molecular</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Genes, Bacterial - genetics</topic><topic>Genomic analysis</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Motility, taxis</topic><topic>Mur enzyme</topic><topic>MurA protein</topic><topic>MurB protein</topic><topic>MurD protein</topic><topic>MurE protein</topic><topic>MurF protein</topic><topic>Nickel</topic><topic>Osmosis</topic><topic>Osmotic pressure</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Peptidoglycan</topic><topic>Peptidoglycan - biosynthesis</topic><topic>Peptidoglycan - genetics</topic><topic>Peptidoglycans</topic><topic>Precursors</topic><topic>Proteins</topic><topic>Pseudomonas aeruginosa</topic><topic>Pseudomonas aeruginosa - enzymology</topic><topic>Pseudomonas aeruginosa - genetics</topic><topic>Pseudomonas aeruginosa - growth & development</topic><topic>Pseudomonas aeruginosa - metabolism</topic><topic>Recombinant Fusion Proteins - 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Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>El Zoeiby, Ahmed</au><au>Sanschagrin, François</au><au>Havugimana, Pierre C.</au><au>Garnier, Alain</au><au>Levesque, Roger C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2001-07</date><risdate>2001</risdate><volume>201</volume><issue>2</issue><spage>229</spage><epage>235</epage><pages>229-235</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
Bacterial peptidoglycan is the cell wall component responsible for maintaining cell integrity against osmotic pressure. Biosynthesis of the cytoplasmic precursor UDP-N-acetylmuramyl pentapeptide is catalyzed by the Mur enzymes. Genomic analysis of the three regions encoding Mur proteins was achieved. We have cloned and over-expressed the murA, -B, -D, -E and -F genes of Pseudomonas aeruginosa in pET expression system by adding a His–Tag to the C-termini of the proteins. Mur proteins were purified to homogeneity by a single chromatographic step on affinity nickel columns. Protein identities were verified through N-terminal sequencing. Enzyme activity was proved by the identification of the pathway's final product.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>11470366</pmid><doi>10.1111/j.1574-6968.2001.tb10761.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2001-07, Vol.201 (2), p.229-235 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Bacterial cell wall Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Biosynthesis Cell Wall - metabolism Cell wall biosynthesis gene Cell walls Chromatography, Affinity Cloning, Molecular Enzymatic activity Enzyme activity Fundamental and applied biological sciences. Psychology Gene expression Genes, Bacterial - genetics Genomic analysis Microbiology Molecular Sequence Data Motility, taxis Mur enzyme MurA protein MurB protein MurD protein MurE protein MurF protein Nickel Osmosis Osmotic pressure Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Peptidoglycan Peptidoglycan - biosynthesis Peptidoglycan - genetics Peptidoglycans Precursors Proteins Pseudomonas aeruginosa Pseudomonas aeruginosa - enzymology Pseudomonas aeruginosa - genetics Pseudomonas aeruginosa - growth & development Pseudomonas aeruginosa - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sequence Analysis, DNA Sequence Analysis, Protein |
| title | In vitro reconstruction of the biosynthetic pathway of peptidoglycan cytoplasmic precursor in Pseudomonas aeruginosa |
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