The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli
The sufABCDSE operon of the Gram-negative bacterium Escherichia coli is induced by oxidative stress and iron deprivation. To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity. Here we report that the SufE...
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| Veröffentlicht in: | The Journal of biological chemistry 2003-11, Vol.278 (46), p.45713-45719 |
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| container_title | The Journal of biological chemistry |
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| creator | Outten, F.Wayne Wood, Matthew J. Muñoz, F.Michael Storz, Gisela |
| description | The sufABCDSE operon of the Gram-negative bacterium Escherichia coli is induced by oxidative stress and iron deprivation. To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity. Here we report that the SufE protein can stimulate the cysteine desulfurase activity of the SufS enzyme up to 8-fold and accepts sulfane sulfur from SufS. This sulfur transfer process from SufS to SufE is sheltered from the environment based on its resistance to added reductants and on the analysis of available crystal structures of the proteins. We also found that the SufB, SufC, and SufD proteins associate in a stable complex and that, in the presence of SufE, the SufBCD complex further stimulates SufS activity up to 32-fold. Thus, the SufE protein and the SufBCD complex act synergistically to modulate the cysteine desulfurase activity of SufS. We propose that this sulfur transfer mechanism may be important for limiting sulfide release during oxidative stress conditions in vivo. |
| doi_str_mv | 10.1074/jbc.M308004200 |
| format | Article |
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To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity. Here we report that the SufE protein can stimulate the cysteine desulfurase activity of the SufS enzyme up to 8-fold and accepts sulfane sulfur from SufS. This sulfur transfer process from SufS to SufE is sheltered from the environment based on its resistance to added reductants and on the analysis of available crystal structures of the proteins. We also found that the SufB, SufC, and SufD proteins associate in a stable complex and that, in the presence of SufE, the SufBCD complex further stimulates SufS activity up to 32-fold. Thus, the SufE protein and the SufBCD complex act synergistically to modulate the cysteine desulfurase activity of SufS. We propose that this sulfur transfer mechanism may be important for limiting sulfide release during oxidative stress conditions in vivo.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M308004200</identifier><identifier>PMID: 12941942</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Carbon-Sulfur Lyases ; Chromatography, Gel ; Cysteine - chemistry ; cysteine desulfurase ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - physiology ; iron-sulfur ; Iron-Sulfur Proteins ; Lyases - chemistry ; Lyases - genetics ; Lyases - physiology ; Molecular Sequence Data ; Oxidative Stress ; Plasmids - metabolism ; Sequence Homology, Amino Acid ; SufE protein ; Sulfur - chemistry ; Sulfur - metabolism</subject><ispartof>The Journal of biological chemistry, 2003-11, Vol.278 (46), p.45713-45719</ispartof><rights>2003 © 2003 ASBMB. 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To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity. Here we report that the SufE protein can stimulate the cysteine desulfurase activity of the SufS enzyme up to 8-fold and accepts sulfane sulfur from SufS. This sulfur transfer process from SufS to SufE is sheltered from the environment based on its resistance to added reductants and on the analysis of available crystal structures of the proteins. We also found that the SufB, SufC, and SufD proteins associate in a stable complex and that, in the presence of SufE, the SufBCD complex further stimulates SufS activity up to 32-fold. Thus, the SufE protein and the SufBCD complex act synergistically to modulate the cysteine desulfurase activity of SufS. We propose that this sulfur transfer mechanism may be important for limiting sulfide release during oxidative stress conditions in vivo.</description><subject>Amino Acid Sequence</subject><subject>Carbon-Sulfur Lyases</subject><subject>Chromatography, Gel</subject><subject>Cysteine - chemistry</subject><subject>cysteine desulfurase</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - physiology</subject><subject>iron-sulfur</subject><subject>Iron-Sulfur Proteins</subject><subject>Lyases - chemistry</subject><subject>Lyases - genetics</subject><subject>Lyases - physiology</subject><subject>Molecular Sequence Data</subject><subject>Oxidative Stress</subject><subject>Plasmids - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>SufE protein</subject><subject>Sulfur - chemistry</subject><subject>Sulfur - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhSMEokvhyhH5gLhlsR07ax-XdEuRiqjUReJmOc6YuErixU5a8oP4n3iblXpCzGWkmW-enuZl2VuC1wRv2Me72qy_FlhgzCjGz7IVwaLIC05-PM9WGFOSS8rFWfYqxjuciknyMjsjVDIiGV1lf_YtoNvJ7tBN8CO4AemhQeMy_FRdoMr3hw5-o93Q6sE8jm9RNccjC-gC4tTZKegIaGtGd-_GGemIbnQYkbdIJ_64R_ugh2ghpM3YPugZWR_QJeRJq5uSWEDbGKGvuxklD7toWgjOtE4j4zv3OnthdRfhzamfZ98vd_vqKr_-9vlLtb3ODWN4zIHJ2siiIVIQK7UpuRWFscB4TS3jst6UnOuNLMrC6oZarUFKqykpMBc1N8V59mHRPQT_a4I4qt5FA12nB_BTVBtScEEx_S9IhOQlkTKB6wU0wccYwKpDcL0OsyJYHRNUKUH1lGA6eHdSnuoemif8FFkC3i9A6362Dy6Aqp1P7-oV3QjFSsV4spkwsWCQ_nXvIKhoHKQEm3RiRtV49y8LfwHOk7Zu</recordid><startdate>20031114</startdate><enddate>20031114</enddate><creator>Outten, F.Wayne</creator><creator>Wood, Matthew J.</creator><creator>Muñoz, F.Michael</creator><creator>Storz, Gisela</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>20031114</creationdate><title>The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli</title><author>Outten, F.Wayne ; Wood, Matthew J. ; Muñoz, F.Michael ; Storz, Gisela</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-e49bc93d1981f9ac65f83cfe45b2f459b7655a79363fad2faae99fa213058b5c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Carbon-Sulfur Lyases</topic><topic>Chromatography, Gel</topic><topic>Cysteine - chemistry</topic><topic>cysteine desulfurase</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - physiology</topic><topic>iron-sulfur</topic><topic>Iron-Sulfur Proteins</topic><topic>Lyases - chemistry</topic><topic>Lyases - genetics</topic><topic>Lyases - physiology</topic><topic>Molecular Sequence Data</topic><topic>Oxidative Stress</topic><topic>Plasmids - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>SufE protein</topic><topic>Sulfur - chemistry</topic><topic>Sulfur - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Outten, F.Wayne</creatorcontrib><creatorcontrib>Wood, Matthew J.</creatorcontrib><creatorcontrib>Muñoz, F.Michael</creatorcontrib><creatorcontrib>Storz, Gisela</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Outten, F.Wayne</au><au>Wood, Matthew J.</au><au>Muñoz, F.Michael</au><au>Storz, Gisela</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2003-11-14</date><risdate>2003</risdate><volume>278</volume><issue>46</issue><spage>45713</spage><epage>45719</epage><pages>45713-45719</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The sufABCDSE operon of the Gram-negative bacterium Escherichia coli is induced by oxidative stress and iron deprivation. To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity. Here we report that the SufE protein can stimulate the cysteine desulfurase activity of the SufS enzyme up to 8-fold and accepts sulfane sulfur from SufS. This sulfur transfer process from SufS to SufE is sheltered from the environment based on its resistance to added reductants and on the analysis of available crystal structures of the proteins. We also found that the SufB, SufC, and SufD proteins associate in a stable complex and that, in the presence of SufE, the SufBCD complex further stimulates SufS activity up to 32-fold. Thus, the SufE protein and the SufBCD complex act synergistically to modulate the cysteine desulfurase activity of SufS. 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| subjects | Amino Acid Sequence Carbon-Sulfur Lyases Chromatography, Gel Cysteine - chemistry cysteine desulfurase Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - physiology iron-sulfur Iron-Sulfur Proteins Lyases - chemistry Lyases - genetics Lyases - physiology Molecular Sequence Data Oxidative Stress Plasmids - metabolism Sequence Homology, Amino Acid SufE protein Sulfur - chemistry Sulfur - metabolism |
| title | The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli |
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