The Quorum-Quenching Lactonase from Bacillus thuringiensis Is a Metalloprotein
Lactonases from Bacillus species hydrolyze the N-acylhomoserine lactone (AHL) signaling molecules used in quorum-sensing pathways of many Gram-negative bacteria, including Pseudomonas aeruginosa and Erwinia carotovora, both significant pathogens. Because of sequence similarity, these AHL lactonases...
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| Veröffentlicht in: | Biochemistry (Easton) 2005-05, Vol.44 (20), p.7559-7569 |
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| creator | Thomas, Pei W Stone, Everett M Costello, Alison L Tierney, David L Fast, Walter |
| description | Lactonases from Bacillus species hydrolyze the N-acylhomoserine lactone (AHL) signaling molecules used in quorum-sensing pathways of many Gram-negative bacteria, including Pseudomonas aeruginosa and Erwinia carotovora, both significant pathogens. Because of sequence similarity, these AHL lactonases have been assigned to the metallo-β-lactamase superfamily of proteins, which includes metalloenzymes of diverse activity, mechanism, and metal content. However, a recent study claims that AHL lactonase from Bacillus sp. 240B1 is not a metalloprotein [Wang, L. H., et al. (2004) J. Biol. Chem. 279, 13645]. Here, the gene for an AHL lactonase from Bacillus thuringiensis is cloned, and the protein is expressed, purified, and found to bind 2 equiv of zinc. The metal-bound form of AHL lactonase catalyzes the hydrolysis of N-hexanoyl-(S)-homoserine lactone but not the (R) enantiomer. Removal of both zinc ions results in loss of activity, and reconstitution with zinc restores activity, indicating the importance of metal ions for catalytic activity. Metal content, sequence alignments, and X-ray absorption spectroscopy of the zinc-containing lactonase all support a proposed dinuclear zinc binding site similar to that found in glyoxalase II. |
| doi_str_mv | 10.1021/bi050050m |
| format | Article |
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Because of sequence similarity, these AHL lactonases have been assigned to the metallo-β-lactamase superfamily of proteins, which includes metalloenzymes of diverse activity, mechanism, and metal content. However, a recent study claims that AHL lactonase from Bacillus sp. 240B1 is not a metalloprotein [Wang, L. H., et al. (2004) J. Biol. Chem. 279, 13645]. Here, the gene for an AHL lactonase from Bacillus thuringiensis is cloned, and the protein is expressed, purified, and found to bind 2 equiv of zinc. The metal-bound form of AHL lactonase catalyzes the hydrolysis of N-hexanoyl-(S)-homoserine lactone but not the (R) enantiomer. Removal of both zinc ions results in loss of activity, and reconstitution with zinc restores activity, indicating the importance of metal ions for catalytic activity. Metal content, sequence alignments, and X-ray absorption spectroscopy of the zinc-containing lactonase all support a proposed dinuclear zinc binding site similar to that found in glyoxalase II.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi050050m</identifier><identifier>PMID: 15895999</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Sequence ; Apoenzymes - chemistry ; Apoenzymes - metabolism ; Bacillus thuringiensis ; Bacillus thuringiensis - enzymology ; Bacillus thuringiensis - genetics ; Bacillus thuringiensis - pathogenicity ; Binding Sites - genetics ; Carboxylic Ester Hydrolases - chemistry ; Carboxylic Ester Hydrolases - genetics ; Carboxylic Ester Hydrolases - isolation & purification ; Carboxylic Ester Hydrolases - physiology ; Carrier Proteins - metabolism ; Cloning, Molecular ; Dialysis ; Enzyme Activation ; Erwinia carotovora ; Kinetics ; Maltose-Binding Proteins ; Metalloproteins - chemistry ; Metalloproteins - genetics ; Metalloproteins - isolation & purification ; Metalloproteins - physiology ; Molecular Sequence Data ; Pseudomonas aeruginosa ; Signal Transduction ; Spectrum Analysis ; X-Rays ; Zinc - chemistry ; Zinc - metabolism</subject><ispartof>Biochemistry (Easton), 2005-05, Vol.44 (20), p.7559-7569</ispartof><rights>Copyright © 2005 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a382t-910e3dda661ef05a594c6fc5ca3be74ff90160caf120985968388d1673b892823</citedby><cites>FETCH-LOGICAL-a382t-910e3dda661ef05a594c6fc5ca3be74ff90160caf120985968388d1673b892823</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi050050m$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi050050m$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15895999$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thomas, Pei W</creatorcontrib><creatorcontrib>Stone, Everett M</creatorcontrib><creatorcontrib>Costello, Alison L</creatorcontrib><creatorcontrib>Tierney, David L</creatorcontrib><creatorcontrib>Fast, Walter</creatorcontrib><title>The Quorum-Quenching Lactonase from Bacillus thuringiensis Is a Metalloprotein</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Lactonases from Bacillus species hydrolyze the N-acylhomoserine lactone (AHL) signaling molecules used in quorum-sensing pathways of many Gram-negative bacteria, including Pseudomonas aeruginosa and Erwinia carotovora, both significant pathogens. Because of sequence similarity, these AHL lactonases have been assigned to the metallo-β-lactamase superfamily of proteins, which includes metalloenzymes of diverse activity, mechanism, and metal content. However, a recent study claims that AHL lactonase from Bacillus sp. 240B1 is not a metalloprotein [Wang, L. H., et al. (2004) J. Biol. Chem. 279, 13645]. Here, the gene for an AHL lactonase from Bacillus thuringiensis is cloned, and the protein is expressed, purified, and found to bind 2 equiv of zinc. The metal-bound form of AHL lactonase catalyzes the hydrolysis of N-hexanoyl-(S)-homoserine lactone but not the (R) enantiomer. Removal of both zinc ions results in loss of activity, and reconstitution with zinc restores activity, indicating the importance of metal ions for catalytic activity. Metal content, sequence alignments, and X-ray absorption spectroscopy of the zinc-containing lactonase all support a proposed dinuclear zinc binding site similar to that found in glyoxalase II.</description><subject>Amino Acid Sequence</subject><subject>Apoenzymes - chemistry</subject><subject>Apoenzymes - metabolism</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - enzymology</subject><subject>Bacillus thuringiensis - genetics</subject><subject>Bacillus thuringiensis - pathogenicity</subject><subject>Binding Sites - genetics</subject><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Carboxylic Ester Hydrolases - genetics</subject><subject>Carboxylic Ester Hydrolases - isolation & purification</subject><subject>Carboxylic Ester Hydrolases - physiology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cloning, Molecular</subject><subject>Dialysis</subject><subject>Enzyme Activation</subject><subject>Erwinia carotovora</subject><subject>Kinetics</subject><subject>Maltose-Binding Proteins</subject><subject>Metalloproteins - chemistry</subject><subject>Metalloproteins - genetics</subject><subject>Metalloproteins - isolation & purification</subject><subject>Metalloproteins - physiology</subject><subject>Molecular Sequence Data</subject><subject>Pseudomonas aeruginosa</subject><subject>Signal Transduction</subject><subject>Spectrum Analysis</subject><subject>X-Rays</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0EtLAzEQB_AgitbHwS8ge1HwsJrHJpscbbFarO_qwUvIplkb3UdNNqDf3khLvQjCQBjmx0z4A7CP4AmCGJ0WFlIYq14DPUQxTDMh6DroQQhZigWDW2Db-7fYZjDPNsEWolxQIUQP3ExmJrkPrQt1eh9Mo2e2eU3GSndto7xJStfWSV9pW1XBJ90suDi3pvHWJyOfqOTadKqq2rlrO2ObXbBRqsqbveW7A56G55PBZTq-vRgNzsapIhx3qUDQkOlUMYZMCamiItOs1FQrUpg8K0sBEYNalQhDwalgnHA-RSwnBReYY7IDjhZ7492PYHwna-u1qSrVmDZ4yXJOUEbJvxDlhGUUowiPF1C71ntnSjl3tlbuSyIof1KWq5SjPVguDUVtpr9yGWsE6QJY35nP1Vy59_gzklM5uXuUD1f4uT_M-_Il-sOFV9rLtza4Job3x-FvOfmR5w</recordid><startdate>20050524</startdate><enddate>20050524</enddate><creator>Thomas, Pei W</creator><creator>Stone, Everett M</creator><creator>Costello, Alison L</creator><creator>Tierney, David L</creator><creator>Fast, Walter</creator><general>American Chemical Society</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20050524</creationdate><title>The Quorum-Quenching Lactonase from Bacillus thuringiensis Is a Metalloprotein</title><author>Thomas, Pei W ; Stone, Everett M ; Costello, Alison L ; Tierney, David L ; Fast, Walter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a382t-910e3dda661ef05a594c6fc5ca3be74ff90160caf120985968388d1673b892823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Apoenzymes - chemistry</topic><topic>Apoenzymes - metabolism</topic><topic>Bacillus thuringiensis</topic><topic>Bacillus thuringiensis - enzymology</topic><topic>Bacillus thuringiensis - genetics</topic><topic>Bacillus thuringiensis - pathogenicity</topic><topic>Binding Sites - genetics</topic><topic>Carboxylic Ester Hydrolases - chemistry</topic><topic>Carboxylic Ester Hydrolases - genetics</topic><topic>Carboxylic Ester Hydrolases - isolation & purification</topic><topic>Carboxylic Ester Hydrolases - physiology</topic><topic>Carrier Proteins - metabolism</topic><topic>Cloning, Molecular</topic><topic>Dialysis</topic><topic>Enzyme Activation</topic><topic>Erwinia carotovora</topic><topic>Kinetics</topic><topic>Maltose-Binding Proteins</topic><topic>Metalloproteins - chemistry</topic><topic>Metalloproteins - genetics</topic><topic>Metalloproteins - isolation & purification</topic><topic>Metalloproteins - physiology</topic><topic>Molecular Sequence Data</topic><topic>Pseudomonas aeruginosa</topic><topic>Signal Transduction</topic><topic>Spectrum Analysis</topic><topic>X-Rays</topic><topic>Zinc - chemistry</topic><topic>Zinc - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thomas, Pei W</creatorcontrib><creatorcontrib>Stone, Everett M</creatorcontrib><creatorcontrib>Costello, Alison L</creatorcontrib><creatorcontrib>Tierney, David L</creatorcontrib><creatorcontrib>Fast, Walter</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thomas, Pei W</au><au>Stone, Everett M</au><au>Costello, Alison L</au><au>Tierney, David L</au><au>Fast, Walter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Quorum-Quenching Lactonase from Bacillus thuringiensis Is a Metalloprotein</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2005-05-24</date><risdate>2005</risdate><volume>44</volume><issue>20</issue><spage>7559</spage><epage>7569</epage><pages>7559-7569</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Lactonases from Bacillus species hydrolyze the N-acylhomoserine lactone (AHL) signaling molecules used in quorum-sensing pathways of many Gram-negative bacteria, including Pseudomonas aeruginosa and Erwinia carotovora, both significant pathogens. Because of sequence similarity, these AHL lactonases have been assigned to the metallo-β-lactamase superfamily of proteins, which includes metalloenzymes of diverse activity, mechanism, and metal content. However, a recent study claims that AHL lactonase from Bacillus sp. 240B1 is not a metalloprotein [Wang, L. H., et al. (2004) J. Biol. Chem. 279, 13645]. Here, the gene for an AHL lactonase from Bacillus thuringiensis is cloned, and the protein is expressed, purified, and found to bind 2 equiv of zinc. The metal-bound form of AHL lactonase catalyzes the hydrolysis of N-hexanoyl-(S)-homoserine lactone but not the (R) enantiomer. Removal of both zinc ions results in loss of activity, and reconstitution with zinc restores activity, indicating the importance of metal ions for catalytic activity. 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| subjects | Amino Acid Sequence Apoenzymes - chemistry Apoenzymes - metabolism Bacillus thuringiensis Bacillus thuringiensis - enzymology Bacillus thuringiensis - genetics Bacillus thuringiensis - pathogenicity Binding Sites - genetics Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - genetics Carboxylic Ester Hydrolases - isolation & purification Carboxylic Ester Hydrolases - physiology Carrier Proteins - metabolism Cloning, Molecular Dialysis Enzyme Activation Erwinia carotovora Kinetics Maltose-Binding Proteins Metalloproteins - chemistry Metalloproteins - genetics Metalloproteins - isolation & purification Metalloproteins - physiology Molecular Sequence Data Pseudomonas aeruginosa Signal Transduction Spectrum Analysis X-Rays Zinc - chemistry Zinc - metabolism |
| title | The Quorum-Quenching Lactonase from Bacillus thuringiensis Is a Metalloprotein |
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