The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
Magnesium chelatase catalyzes the first essential step in chlorophyll biosynthesis. Results: Mutations in the AAA+ domain of the magnesium chelatase ChlD subunit reduce but do not abolish catalytic activity. Conclusion: ChlD is an allosteric regulator of magnesium chelatase. Significance: These obse...
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| Veröffentlicht in: | The Journal of biological chemistry 2013-10, Vol.288 (40), p.28727-28732 |
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| container_title | The Journal of biological chemistry |
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| creator | Adams, Nathan B.P. Reid, James D. |
| description | Magnesium chelatase catalyzes the first essential step in chlorophyll biosynthesis.
Results: Mutations in the AAA+ domain of the magnesium chelatase ChlD subunit reduce but do not abolish catalytic activity.
Conclusion: ChlD is an allosteric regulator of magnesium chelatase.
Significance: These observations reveal an essential role for the ChlD protein in the first committed stage in chlorophyll biosynthesis.
Magnesium chelatase is an AAA+ ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA+ domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA+ domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg2+ and MgATP2− binding. |
| doi_str_mv | 10.1074/jbc.M113.477943 |
| format | Article |
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Results: Mutations in the AAA+ domain of the magnesium chelatase ChlD subunit reduce but do not abolish catalytic activity.
Conclusion: ChlD is an allosteric regulator of magnesium chelatase.
Significance: These observations reveal an essential role for the ChlD protein in the first committed stage in chlorophyll biosynthesis.
Magnesium chelatase is an AAA+ ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA+ domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA+ domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg2+ and MgATP2− binding.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M113.477943</identifier><identifier>PMID: 23940041</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphate - pharmacology ; Allosteric Regulation ; ATPases ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Biosynthesis ; Circular Dichroism ; Deuteroporphyrins - metabolism ; Enzyme Catalysis ; Enzymology ; Kinetics ; Lyases - chemistry ; Lyases - metabolism ; Mutagenesis Site-specific ; Mutant Proteins - chemistry ; Mutant Proteins - metabolism ; Porphyrin ; Protein Structure, Tertiary ; Structure-Activity Relationship ; Synechocystis ; Synechocystis - enzymology</subject><ispartof>The Journal of biological chemistry, 2013-10, Vol.288 (40), p.28727-28732</ispartof><rights>2013 © 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-55b56ed88d0ae1ceae6be36a110b454f13c5a9275bbb1f83a25fbc7e9bb822b03</citedby><cites>FETCH-LOGICAL-c476t-55b56ed88d0ae1ceae6be36a110b454f13c5a9275bbb1f83a25fbc7e9bb822b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3789969/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3789969/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23940041$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Adams, Nathan B.P.</creatorcontrib><creatorcontrib>Reid, James D.</creatorcontrib><title>The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Magnesium chelatase catalyzes the first essential step in chlorophyll biosynthesis.
Results: Mutations in the AAA+ domain of the magnesium chelatase ChlD subunit reduce but do not abolish catalytic activity.
Conclusion: ChlD is an allosteric regulator of magnesium chelatase.
Significance: These observations reveal an essential role for the ChlD protein in the first committed stage in chlorophyll biosynthesis.
Magnesium chelatase is an AAA+ ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA+ domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA+ domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg2+ and MgATP2− binding.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Allosteric Regulation</subject><subject>ATPases</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biosynthesis</subject><subject>Circular Dichroism</subject><subject>Deuteroporphyrins - metabolism</subject><subject>Enzyme Catalysis</subject><subject>Enzymology</subject><subject>Kinetics</subject><subject>Lyases - chemistry</subject><subject>Lyases - metabolism</subject><subject>Mutagenesis Site-specific</subject><subject>Mutant Proteins - chemistry</subject><subject>Mutant Proteins - metabolism</subject><subject>Porphyrin</subject><subject>Protein Structure, Tertiary</subject><subject>Structure-Activity Relationship</subject><subject>Synechocystis</subject><subject>Synechocystis - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUFP3DAQha2qVVloz71VPlaqstixndiXSqtQoBKoqFCpN8t2JqxREi92grT_Hi8LqD3Ul7FnvnkezUPoEyVLSmp-fGfd8pJStuR1rTh7gxaUSFYwQf-8RQtCSlqoUsgDdJjSHcmHK_oeHZRM8XynCzTfrAGv-j6kCaJ3-FfoAYcOT7v0avUVn4TB-HGXatb9Cb6KYYL87mIYnqBLcztC8vOQ69CbyaSn_uvtCG4d3DZNPuHrDTgPCV81Da4kYR_Qu870CT4-xyP0-_T7TXNeXPw8-9GsLgrH62oqhLCiglbKlhigDgxUFlhlKCWWC95R5oRRZS2stbSTzJSis64GZa0sS0vYEfq2193MdoDWwThF0-tN9IOJWx2M1_9WRr_Wt-FBs1oqVaks8OVZIIb7GdKkB58c9L0ZIcxJU15xrmoqaUaP96iLIaUI3es3lOidWTqbpXdm6b1ZuePz39O98i_uZEDtAcg7evAQdcprHB20PoKbdBv8f8UfAS4xpA8</recordid><startdate>20131004</startdate><enddate>20131004</enddate><creator>Adams, Nathan B.P.</creator><creator>Reid, James D.</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>M7N</scope><scope>5PM</scope></search><sort><creationdate>20131004</creationdate><title>The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803</title><author>Adams, Nathan B.P. ; Reid, James D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-55b56ed88d0ae1ceae6be36a110b454f13c5a9275bbb1f83a25fbc7e9bb822b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Allosteric Regulation</topic><topic>ATPases</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biosynthesis</topic><topic>Circular Dichroism</topic><topic>Deuteroporphyrins - metabolism</topic><topic>Enzyme Catalysis</topic><topic>Enzymology</topic><topic>Kinetics</topic><topic>Lyases - chemistry</topic><topic>Lyases - metabolism</topic><topic>Mutagenesis Site-specific</topic><topic>Mutant Proteins - chemistry</topic><topic>Mutant Proteins - metabolism</topic><topic>Porphyrin</topic><topic>Protein Structure, Tertiary</topic><topic>Structure-Activity Relationship</topic><topic>Synechocystis</topic><topic>Synechocystis - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Adams, Nathan B.P.</creatorcontrib><creatorcontrib>Reid, James D.</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Adams, Nathan B.P.</au><au>Reid, James D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2013-10-04</date><risdate>2013</risdate><volume>288</volume><issue>40</issue><spage>28727</spage><epage>28732</epage><pages>28727-28732</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Magnesium chelatase catalyzes the first essential step in chlorophyll biosynthesis.
Results: Mutations in the AAA+ domain of the magnesium chelatase ChlD subunit reduce but do not abolish catalytic activity.
Conclusion: ChlD is an allosteric regulator of magnesium chelatase.
Significance: These observations reveal an essential role for the ChlD protein in the first committed stage in chlorophyll biosynthesis.
Magnesium chelatase is an AAA+ ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA+ domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA+ domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg2+ and MgATP2− binding.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>23940041</pmid><doi>10.1074/jbc.M113.477943</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - pharmacology Allosteric Regulation ATPases Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biosynthesis Circular Dichroism Deuteroporphyrins - metabolism Enzyme Catalysis Enzymology Kinetics Lyases - chemistry Lyases - metabolism Mutagenesis Site-specific Mutant Proteins - chemistry Mutant Proteins - metabolism Porphyrin Protein Structure, Tertiary Structure-Activity Relationship Synechocystis Synechocystis - enzymology |
| title | The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803 |
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