Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis
Plastocyanin is synthesized in the cytoplasm as a larger precursor and transported across three membranes into the chloroplast thylakoid lumen. Processing to the mature size involves successive cleavages by a stromal and a thylakoidal peptidase. In this report we describe the partial purification an...
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| Veröffentlicht in: | The Journal of biological chemistry 1987-12, Vol.262 (34), p.16386-16390 |
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| creator | Kirwin, PM Elderfield, PD Robinson, C |
| description | Plastocyanin is synthesized in the cytoplasm as a larger precursor and transported across three membranes into the chloroplast thylakoid lumen. Processing to the mature size involves successive cleavages by a stromal and a thylakoidal peptidase. In this report we describe the partial purification and characterization of the thylakoidal peptidase involved. The enzyme has been purified 36-fold from Pisum sativum thylakoids after solubilization using Triton X-100. The peptidase processes the plastocyanin import intermediate to the mature size, but no further, and is capable of processing pre-plastocyanin to the mature size but at a lower rate. No detectable activity is displayed against non-chloroplast proteins or precursors of stromal proteins. The enzyme has a pH optimum of 6.5-7 and is activated by chelating agents such as EDTA and EGTA. No inhibitors of the peptidase have been found to date. |
| doi_str_mv | 10.1016/S0021-9258(18)49267-8 |
| format | Article |
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The peptidase processes the plastocyanin import intermediate to the mature size, but no further, and is capable of processing pre-plastocyanin to the mature size but at a lower rate. No detectable activity is displayed against non-chloroplast proteins or precursors of stromal proteins. The enzyme has a pH optimum of 6.5-7 and is activated by chelating agents such as EDTA and EGTA. No inhibitors of the peptidase have been found to date.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)49267-8</identifier><identifier>PMID: 3316219</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Biological and medical sciences ; Biological Transport, Active ; Cell physiology ; chloroplasts ; Chloroplasts - metabolism ; EPURATION ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Membrane and intracellular transports ; Molecular and cellular biology ; peptidase ; Peptide Hydrolases - isolation & purification ; Peptide Hydrolases - metabolism ; PIGMENT ; PIGMENTOS ; PIGMENTS ; PISUM SATIVUM ; PLANT PROTEINS ; Plant Proteins - biosynthesis ; Plant Proteins - metabolism ; Plants - enzymology ; PLASTE ; PLASTIDIOS ; PLASTIDS ; plastocyanin ; Plastocyanin - biosynthesis ; PROTEIN SYNTHESIS ; PROTEINAS VEGETALES ; PROTEINE VEGETALE ; PURIFICACION ; PURIFICATION ; SINTESIS DE PROTEINAS ; SYNTHESE PROTEIQUE</subject><ispartof>The Journal of biological chemistry, 1987-12, Vol.262 (34), p.16386-16390</ispartof><rights>1987 © 1987 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c517t-12e692d37df216e9e396fbaae4f871f5df62dfd130aa3517c49ea65fc7011be03</citedby><cites>FETCH-LOGICAL-c517t-12e692d37df216e9e396fbaae4f871f5df62dfd130aa3517c49ea65fc7011be03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7616074$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3316219$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kirwin, PM</creatorcontrib><creatorcontrib>Elderfield, PD</creatorcontrib><creatorcontrib>Robinson, C</creatorcontrib><title>Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Plastocyanin is synthesized in the cytoplasm as a larger precursor and transported across three membranes into the chloroplast thylakoid lumen. Processing to the mature size involves successive cleavages by a stromal and a thylakoidal peptidase. In this report we describe the partial purification and characterization of the thylakoidal peptidase involved. The enzyme has been purified 36-fold from Pisum sativum thylakoids after solubilization using Triton X-100. The peptidase processes the plastocyanin import intermediate to the mature size, but no further, and is capable of processing pre-plastocyanin to the mature size but at a lower rate. No detectable activity is displayed against non-chloroplast proteins or precursors of stromal proteins. The enzyme has a pH optimum of 6.5-7 and is activated by chelating agents such as EDTA and EGTA. No inhibitors of the peptidase have been found to date.</description><subject>Biological and medical sciences</subject><subject>Biological Transport, Active</subject><subject>Cell physiology</subject><subject>chloroplasts</subject><subject>Chloroplasts - metabolism</subject><subject>EPURATION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Membrane and intracellular transports</subject><subject>Molecular and cellular biology</subject><subject>peptidase</subject><subject>Peptide Hydrolases - isolation & purification</subject><subject>Peptide Hydrolases - metabolism</subject><subject>PIGMENT</subject><subject>PIGMENTOS</subject><subject>PIGMENTS</subject><subject>PISUM SATIVUM</subject><subject>PLANT PROTEINS</subject><subject>Plant Proteins - biosynthesis</subject><subject>Plant Proteins - metabolism</subject><subject>Plants - enzymology</subject><subject>PLASTE</subject><subject>PLASTIDIOS</subject><subject>PLASTIDS</subject><subject>plastocyanin</subject><subject>Plastocyanin - biosynthesis</subject><subject>PROTEIN SYNTHESIS</subject><subject>PROTEINAS VEGETALES</subject><subject>PROTEINE VEGETALE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>SINTESIS DE PROTEINAS</subject><subject>SYNTHESE PROTEIQUE</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhSMEKtPCG1ApC4TKIsXXjh1nhVDFn1QJpLYSO8vjXE8MmTjYnkHzBLw2zsxoWNYb_5zvHtv3FMUlkGsgIN7dEUKhaimXVyDf1i0VTSWfFAsgklWMw4-nxeKEPC_OY_xJ8qhbOCvOGANBoV0Uf--DHuPkQyq9LafgE7oxlm5MvjT94IOfBh1TvC6_65CcHsppE5x1Rifnx7lGl6nfDfqXd92sBm8wRjeuygmnlM8iZretH7bY5UW5t_Nmp8e8WTq_whGjiy-KZ1YPEV8e54vi4dPH-5sv1e23z19vPtxWhkOTKqAoWtqxprMUBLbIWmGXWmNtZQOWd1bQznbAiNa5B42pW9SCW9MQgCUSdlG8Ofjmh_7eYExq7aLBYdAj-k1UTSNrxgl_FAQORHBOM8gPoAk-xoBWTcGtddgpIGpOSu2TUnMMCqTaJ6Vkrrs8XrBZrrE7VR2jyfrro66j0YPNORkXT1gjQJCm_o_1btX_cQFVbqrpca2ooIrVCgSTImOvDpjVXulVyE4Pd1ICCJByfsz7g4y591uHQUXjcDTYZUeTVOfdI9_5B4h_yBE</recordid><startdate>19871205</startdate><enddate>19871205</enddate><creator>Kirwin, PM</creator><creator>Elderfield, PD</creator><creator>Robinson, C</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19871205</creationdate><title>Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis</title><author>Kirwin, PM ; Elderfield, PD ; Robinson, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c517t-12e692d37df216e9e396fbaae4f871f5df62dfd130aa3517c49ea65fc7011be03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Biological and medical sciences</topic><topic>Biological Transport, Active</topic><topic>Cell physiology</topic><topic>chloroplasts</topic><topic>Chloroplasts - metabolism</topic><topic>EPURATION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Membrane and intracellular transports</topic><topic>Molecular and cellular biology</topic><topic>peptidase</topic><topic>Peptide Hydrolases - isolation & purification</topic><topic>Peptide Hydrolases - metabolism</topic><topic>PIGMENT</topic><topic>PIGMENTOS</topic><topic>PIGMENTS</topic><topic>PISUM SATIVUM</topic><topic>PLANT PROTEINS</topic><topic>Plant Proteins - biosynthesis</topic><topic>Plant Proteins - metabolism</topic><topic>Plants - enzymology</topic><topic>PLASTE</topic><topic>PLASTIDIOS</topic><topic>PLASTIDS</topic><topic>plastocyanin</topic><topic>Plastocyanin - biosynthesis</topic><topic>PROTEIN SYNTHESIS</topic><topic>PROTEINAS VEGETALES</topic><topic>PROTEINE VEGETALE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>SINTESIS DE PROTEINAS</topic><topic>SYNTHESE PROTEIQUE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kirwin, PM</creatorcontrib><creatorcontrib>Elderfield, PD</creatorcontrib><creatorcontrib>Robinson, C</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Pascal-Francis</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</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>Kirwin, PM</au><au>Elderfield, PD</au><au>Robinson, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1987-12-05</date><risdate>1987</risdate><volume>262</volume><issue>34</issue><spage>16386</spage><epage>16390</epage><pages>16386-16390</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Plastocyanin is synthesized in the cytoplasm as a larger precursor and transported across three membranes into the chloroplast thylakoid lumen. Processing to the mature size involves successive cleavages by a stromal and a thylakoidal peptidase. In this report we describe the partial purification and characterization of the thylakoidal peptidase involved. The enzyme has been purified 36-fold from Pisum sativum thylakoids after solubilization using Triton X-100. The peptidase processes the plastocyanin import intermediate to the mature size, but no further, and is capable of processing pre-plastocyanin to the mature size but at a lower rate. No detectable activity is displayed against non-chloroplast proteins or precursors of stromal proteins. The enzyme has a pH optimum of 6.5-7 and is activated by chelating agents such as EDTA and EGTA. No inhibitors of the peptidase have been found to date.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3316219</pmid><doi>10.1016/S0021-9258(18)49267-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1987-12, Vol.262 (34), p.16386-16390 |
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| source | MEDLINE; Free E-Journal (出版社公開部分のみ）; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Biological Transport, Active Cell physiology chloroplasts Chloroplasts - metabolism EPURATION Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Membrane and intracellular transports Molecular and cellular biology peptidase Peptide Hydrolases - isolation & purification Peptide Hydrolases - metabolism PIGMENT PIGMENTOS PIGMENTS PISUM SATIVUM PLANT PROTEINS Plant Proteins - biosynthesis Plant Proteins - metabolism Plants - enzymology PLASTE PLASTIDIOS PLASTIDS plastocyanin Plastocyanin - biosynthesis PROTEIN SYNTHESIS PROTEINAS VEGETALES PROTEINE VEGETALE PURIFICACION PURIFICATION SINTESIS DE PROTEINAS SYNTHESE PROTEIQUE |
| title | Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis |
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