NblA from Anabaena sp. PCC 7120 is a mostly α‐helical protein undergoing reversible trimerization in solution
The nblA family of genes encodes for small proteins necessary for the ordered degradation of phycobilisomes under certain stress conditions, a process known as chlorosis. Genes homologous to nblA seem to occur in all phycobilisome‐containing organisms. However, to date, no molecular mechanism is kno...
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| Veröffentlicht in: | European journal of biochemistry 2002-09, Vol.269 (18), p.4617-4624 |
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| container_title | European journal of biochemistry |
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| creator | Strauss, Holger Misselwitz, Rolf Labudde, Dirk Nicklisch, Sabine Baier, Kerstin |
| description | The nblA family of genes encodes for small proteins necessary for the ordered degradation of phycobilisomes under certain stress conditions, a process known as chlorosis. Genes homologous to nblA seem to occur in all phycobilisome‐containing organisms. However, to date, no molecular mechanism is known for the action of NblA, nor have the gene products been characterized to understand the physical properties of the molecule and thus help elucidate the mechanism on a structural basis.
In this study we report on the first characterization of an NblA‐homologous gene product. The chromosomal gene from the cyanobacterium Anabaena sp. PCC 7120 was cloned, heterologously expressed in Escherichia coli and purified to apparent homogeneity. This allowed the protein to be characterized by analytical ultracentrifugation and CD spectroscopy. These experiments show that the NblA protein has a mostly α‐helical structure, undergoing an association reaction of folded monomers to form trimers in solution. No dimers are detectable. |
| doi_str_mv | 10.1046/j.1432-1033.2002.03161.x |
| format | Article |
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In this study we report on the first characterization of an NblA‐homologous gene product. The chromosomal gene from the cyanobacterium Anabaena sp. PCC 7120 was cloned, heterologously expressed in Escherichia coli and purified to apparent homogeneity. This allowed the protein to be characterized by analytical ultracentrifugation and CD spectroscopy. These experiments show that the NblA protein has a mostly α‐helical structure, undergoing an association reaction of folded monomers to form trimers in solution. No dimers are detectable.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1046/j.1432-1033.2002.03161.x</identifier><identifier>PMID: 12230574</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Anabaena ; Anabaena - chemistry ; analytical ultracentrifugation ; Bacterial Proteins - chemistry ; chlorosis ; Circular Dichroism ; Cold Temperature ; cyanobacteria ; Cyanophyta ; Hot Temperature ; NblA ; nblA gene ; NblA protein ; phycobilisome ; Phycobilisomes ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Spectrometry, Fluorescence ; Ultracentrifugation</subject><ispartof>European journal of biochemistry, 2002-09, Vol.269 (18), p.4617-4624</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3971-8fc7c2aac1eb323207725a512c5c7acb010348bc40e6f457d14667fe7a91018d3</citedby><cites>FETCH-LOGICAL-c3971-8fc7c2aac1eb323207725a512c5c7acb010348bc40e6f457d14667fe7a91018d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1432-1033.2002.03161.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1432-1033.2002.03161.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12230574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Strauss, Holger</creatorcontrib><creatorcontrib>Misselwitz, Rolf</creatorcontrib><creatorcontrib>Labudde, Dirk</creatorcontrib><creatorcontrib>Nicklisch, Sabine</creatorcontrib><creatorcontrib>Baier, Kerstin</creatorcontrib><title>NblA from Anabaena sp. PCC 7120 is a mostly α‐helical protein undergoing reversible trimerization in solution</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The nblA family of genes encodes for small proteins necessary for the ordered degradation of phycobilisomes under certain stress conditions, a process known as chlorosis. Genes homologous to nblA seem to occur in all phycobilisome‐containing organisms. However, to date, no molecular mechanism is known for the action of NblA, nor have the gene products been characterized to understand the physical properties of the molecule and thus help elucidate the mechanism on a structural basis.
In this study we report on the first characterization of an NblA‐homologous gene product. The chromosomal gene from the cyanobacterium Anabaena sp. PCC 7120 was cloned, heterologously expressed in Escherichia coli and purified to apparent homogeneity. This allowed the protein to be characterized by analytical ultracentrifugation and CD spectroscopy. These experiments show that the NblA protein has a mostly α‐helical structure, undergoing an association reaction of folded monomers to form trimers in solution. No dimers are detectable.</description><subject>Anabaena</subject><subject>Anabaena - chemistry</subject><subject>analytical ultracentrifugation</subject><subject>Bacterial Proteins - chemistry</subject><subject>chlorosis</subject><subject>Circular Dichroism</subject><subject>Cold Temperature</subject><subject>cyanobacteria</subject><subject>Cyanophyta</subject><subject>Hot Temperature</subject><subject>NblA</subject><subject>nblA gene</subject><subject>NblA protein</subject><subject>phycobilisome</subject><subject>Phycobilisomes</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Spectrometry, Fluorescence</subject><subject>Ultracentrifugation</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9O3DAUxi3UCqbAFSqv2CV9thM72SBNR0ArIajUdm05nhfqkZMMdtIyrJB6gV6lF-khOAkJM6LLdvU-6f3e348QyiBlkMl3q5RlgicMhEg5AE9BMMnSuz0ye0m8IjMAliW8zOUBeRPjCgBkKdU-OWCcC8hVNiPhqvJzWoeuofPWVAZbQ-M6pZ8Wi8eHn4pxoC5SQ5su9n5D__x-fPj1Db2zxtN16Hp0LR3aJYabzrU3NOB3DNFVHmkfXIPB3ZvedS0dsdj5YdJH5HVtfMTjXTwkX8_Pviw-JJfXFx8X88vEilKxpKitstwYy7ASXHBQiucmZ9zmVhlbwXhkVlQ2A5R1lqsly6RUNSpTMmDFUhySk23fcc_bAWOvGxctem9a7IaoFYdSKFn8E2SFLFSRwwgWW9CGLsaAtV6PR5qw0Qz0ZIxe6en_evq_nozRz8bou7H07W7GUDW4_Fu4c2IETrfAD-dx89-N9fnZ-8-TFE8i7J5F</recordid><startdate>200209</startdate><enddate>200209</enddate><creator>Strauss, Holger</creator><creator>Misselwitz, Rolf</creator><creator>Labudde, Dirk</creator><creator>Nicklisch, Sabine</creator><creator>Baier, Kerstin</creator><general>Blackwell Science Ltd</general><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>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>200209</creationdate><title>NblA from Anabaena sp. PCC 7120 is a mostly α‐helical protein undergoing reversible trimerization in solution</title><author>Strauss, Holger ; Misselwitz, Rolf ; Labudde, Dirk ; Nicklisch, Sabine ; Baier, Kerstin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3971-8fc7c2aac1eb323207725a512c5c7acb010348bc40e6f457d14667fe7a91018d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Anabaena</topic><topic>Anabaena - chemistry</topic><topic>analytical ultracentrifugation</topic><topic>Bacterial Proteins - chemistry</topic><topic>chlorosis</topic><topic>Circular Dichroism</topic><topic>Cold Temperature</topic><topic>cyanobacteria</topic><topic>Cyanophyta</topic><topic>Hot Temperature</topic><topic>NblA</topic><topic>nblA gene</topic><topic>NblA protein</topic><topic>phycobilisome</topic><topic>Phycobilisomes</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Secondary</topic><topic>Spectrometry, Fluorescence</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Strauss, Holger</creatorcontrib><creatorcontrib>Misselwitz, Rolf</creatorcontrib><creatorcontrib>Labudde, Dirk</creatorcontrib><creatorcontrib>Nicklisch, Sabine</creatorcontrib><creatorcontrib>Baier, Kerstin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Strauss, Holger</au><au>Misselwitz, Rolf</au><au>Labudde, Dirk</au><au>Nicklisch, Sabine</au><au>Baier, Kerstin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NblA from Anabaena sp. PCC 7120 is a mostly α‐helical protein undergoing reversible trimerization in solution</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2002-09</date><risdate>2002</risdate><volume>269</volume><issue>18</issue><spage>4617</spage><epage>4624</epage><pages>4617-4624</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The nblA family of genes encodes for small proteins necessary for the ordered degradation of phycobilisomes under certain stress conditions, a process known as chlorosis. Genes homologous to nblA seem to occur in all phycobilisome‐containing organisms. However, to date, no molecular mechanism is known for the action of NblA, nor have the gene products been characterized to understand the physical properties of the molecule and thus help elucidate the mechanism on a structural basis.
In this study we report on the first characterization of an NblA‐homologous gene product. The chromosomal gene from the cyanobacterium Anabaena sp. PCC 7120 was cloned, heterologously expressed in Escherichia coli and purified to apparent homogeneity. This allowed the protein to be characterized by analytical ultracentrifugation and CD spectroscopy. These experiments show that the NblA protein has a mostly α‐helical structure, undergoing an association reaction of folded monomers to form trimers in solution. No dimers are detectable.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>12230574</pmid><doi>10.1046/j.1432-1033.2002.03161.x</doi><tpages>8</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 2002-09, Vol.269 (18), p.4617-4624 |
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| source | MEDLINE; Wiley Journals; Alma/SFX Local Collection |
| subjects | Anabaena Anabaena - chemistry analytical ultracentrifugation Bacterial Proteins - chemistry chlorosis Circular Dichroism Cold Temperature cyanobacteria Cyanophyta Hot Temperature NblA nblA gene NblA protein phycobilisome Phycobilisomes Protein Structure, Quaternary Protein Structure, Secondary Spectrometry, Fluorescence Ultracentrifugation |
| title | NblA from Anabaena sp. PCC 7120 is a mostly α‐helical protein undergoing reversible trimerization in solution |
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