Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii
The hydrogenase enzyme occurring in Chlamydomonas reinhardtii is induced by anaerobic adaptation of the cells. In aerobically growing cells, antibodies against the hydrogenase failed to detect either active or inactive enzyme. However, already 10 min after the onset of anaerobic adaptation, the prot...
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Veröffentlicht in: | European journal of biochemistry 1994-06, Vol.222 (3), p.769-774 |
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description | The hydrogenase enzyme occurring in Chlamydomonas reinhardtii is induced by anaerobic adaptation of the cells. In aerobically growing cells, antibodies against the hydrogenase failed to detect either active or inactive enzyme. However, already 10 min after the onset of anaerobic adaptation, the protein could be detected. The maximal amount of enzyme was reached after 2–3 hours anaerobiosis. Addition of nickel or iron to the growth medium did not influence activity. In atomic absorption experiments, a Ni/Fe ratio of about 1:250 was measured. We, therefore, propose the hydrogenase from C. reinhardtii to be of the Fe‐only type. Adaptation in the presence of uncouplers of phosphorylation showed this process to be energy‐dependent. From protein synthesis inhibition experiments, it is concluded that the protein is synthesized on cytoplasmic ribosomes and, therefore, must be nuclear encoded. After isolation of intact chloroplasts from adapted cells, the active enzyme was shown, by Western‐blotting analysis, to be located in the chloroplasts. |
doi_str_mv | 10.1111/j.1432-1033.1994.tb18923.x |
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Dirk</creator><creatorcontrib>HAPPE, Thomas ; MOSLER, Britta ; NABER, J. Dirk</creatorcontrib><description>The hydrogenase enzyme occurring in Chlamydomonas reinhardtii is induced by anaerobic adaptation of the cells. In aerobically growing cells, antibodies against the hydrogenase failed to detect either active or inactive enzyme. However, already 10 min after the onset of anaerobic adaptation, the protein could be detected. The maximal amount of enzyme was reached after 2–3 hours anaerobiosis. Addition of nickel or iron to the growth medium did not influence activity. In atomic absorption experiments, a Ni/Fe ratio of about 1:250 was measured. We, therefore, propose the hydrogenase from C. reinhardtii to be of the Fe‐only type. Adaptation in the presence of uncouplers of phosphorylation showed this process to be energy‐dependent. From protein synthesis inhibition experiments, it is concluded that the protein is synthesized on cytoplasmic ribosomes and, therefore, must be nuclear encoded. After isolation of intact chloroplasts from adapted cells, the active enzyme was shown, by Western‐blotting analysis, to be located in the chloroplasts.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1994.tb18923.x</identifier><identifier>PMID: 8026490</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adaptation, Physiological ; Anaerobiosis ; Animals ; Blotting, Western ; Chlamydomonas reinhardtii ; Chlamydomonas reinhardtii - enzymology ; Chlamydomonas reinhardtii - growth & development ; Chloramphenicol - pharmacology ; Chloroplasts - enzymology ; Cycloheximide - pharmacology ; Enzyme Induction - drug effects ; Freshwater ; Hydrogenase - analysis ; Hydrogenase - biosynthesis ; Hydrogenase - chemistry ; Iron - analysis ; Iron - pharmacology ; Nickel - pharmacology ; Phosphorylation ; Ribosomes - enzymology ; Spectrophotometry, Atomic ; Uncoupling Agents - pharmacology</subject><ispartof>European journal of biochemistry, 1994-06, Vol.222 (3), p.769-774</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4679-ba5b8e00b4432e71d0a5fb6ee34a4a4105aa3affe72ac6e49890b516083c6ae93</citedby><cites>FETCH-LOGICAL-c4679-ba5b8e00b4432e71d0a5fb6ee34a4a4105aa3affe72ac6e49890b516083c6ae93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8026490$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HAPPE, Thomas</creatorcontrib><creatorcontrib>MOSLER, Britta</creatorcontrib><creatorcontrib>NABER, J. Dirk</creatorcontrib><title>Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The hydrogenase enzyme occurring in Chlamydomonas reinhardtii is induced by anaerobic adaptation of the cells. In aerobically growing cells, antibodies against the hydrogenase failed to detect either active or inactive enzyme. However, already 10 min after the onset of anaerobic adaptation, the protein could be detected. The maximal amount of enzyme was reached after 2–3 hours anaerobiosis. Addition of nickel or iron to the growth medium did not influence activity. In atomic absorption experiments, a Ni/Fe ratio of about 1:250 was measured. We, therefore, propose the hydrogenase from C. reinhardtii to be of the Fe‐only type. Adaptation in the presence of uncouplers of phosphorylation showed this process to be energy‐dependent. From protein synthesis inhibition experiments, it is concluded that the protein is synthesized on cytoplasmic ribosomes and, therefore, must be nuclear encoded. After isolation of intact chloroplasts from adapted cells, the active enzyme was shown, by Western‐blotting analysis, to be located in the chloroplasts.</description><subject>Adaptation, Physiological</subject><subject>Anaerobiosis</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chlamydomonas reinhardtii - enzymology</subject><subject>Chlamydomonas reinhardtii - growth & development</subject><subject>Chloramphenicol - pharmacology</subject><subject>Chloroplasts - enzymology</subject><subject>Cycloheximide - pharmacology</subject><subject>Enzyme Induction - drug effects</subject><subject>Freshwater</subject><subject>Hydrogenase - analysis</subject><subject>Hydrogenase - biosynthesis</subject><subject>Hydrogenase - chemistry</subject><subject>Iron - analysis</subject><subject>Iron - pharmacology</subject><subject>Nickel - pharmacology</subject><subject>Phosphorylation</subject><subject>Ribosomes - enzymology</subject><subject>Spectrophotometry, Atomic</subject><subject>Uncoupling Agents - pharmacology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkUFv1DAQhS1EVbalPwHJ4sCJpOM4cWIuCFZtqVSJA_RsTZLJrldOXOys6PLrcbSrXhGeg2W9b8aa9xh7LyAX6VzvclHKIhMgZS60LvO5FY0uZP78iq1epNdsBSDKrNCVesMuYtwBgNKqPmfnDRSq1LBi_f3U77vZ-ukjd75DZ__g8uI49XykGR3v_DTTNHM_8O2hD35DE0biduLzlvgmECXabZCvtw7HQ-9HnwAeyE5bDP1s7Vt2NqCLdHW6L9nj7c3P9bfs4fvd_frLQ9aVqtZZi1XbEEBbphWoFj1gNbSKSJaYSkCFKHEYqC6wU1TqRkNbCQWN7BSSlpfsw3HuU_C_9hRnM9rYkXM4kd9HU6uqqWXC_wUKpaDWAAn8dAS74GMMNJinYEcMByPALFmYnVkMN4vhZsnCnLIwz6n53emXfTtS_9J6Mj_pn4_6b-vo8B-Tze3N1x-10vIveaCbEw</recordid><startdate>19940615</startdate><enddate>19940615</enddate><creator>HAPPE, Thomas</creator><creator>MOSLER, Britta</creator><creator>NABER, J. Dirk</creator><general>Blackwell Publishing 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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>19940615</creationdate><title>Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii</title><author>HAPPE, Thomas ; MOSLER, Britta ; NABER, J. Dirk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4679-ba5b8e00b4432e71d0a5fb6ee34a4a4105aa3affe72ac6e49890b516083c6ae93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Adaptation, Physiological</topic><topic>Anaerobiosis</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chlamydomonas reinhardtii - enzymology</topic><topic>Chlamydomonas reinhardtii - growth & development</topic><topic>Chloramphenicol - pharmacology</topic><topic>Chloroplasts - enzymology</topic><topic>Cycloheximide - pharmacology</topic><topic>Enzyme Induction - drug effects</topic><topic>Freshwater</topic><topic>Hydrogenase - analysis</topic><topic>Hydrogenase - biosynthesis</topic><topic>Hydrogenase - chemistry</topic><topic>Iron - analysis</topic><topic>Iron - pharmacology</topic><topic>Nickel - pharmacology</topic><topic>Phosphorylation</topic><topic>Ribosomes - enzymology</topic><topic>Spectrophotometry, Atomic</topic><topic>Uncoupling Agents - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HAPPE, Thomas</creatorcontrib><creatorcontrib>MOSLER, Britta</creatorcontrib><creatorcontrib>NABER, J. Dirk</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HAPPE, Thomas</au><au>MOSLER, Britta</au><au>NABER, J. Dirk</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1994-06-15</date><risdate>1994</risdate><volume>222</volume><issue>3</issue><spage>769</spage><epage>774</epage><pages>769-774</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The hydrogenase enzyme occurring in Chlamydomonas reinhardtii is induced by anaerobic adaptation of the cells. In aerobically growing cells, antibodies against the hydrogenase failed to detect either active or inactive enzyme. However, already 10 min after the onset of anaerobic adaptation, the protein could be detected. The maximal amount of enzyme was reached after 2–3 hours anaerobiosis. Addition of nickel or iron to the growth medium did not influence activity. In atomic absorption experiments, a Ni/Fe ratio of about 1:250 was measured. We, therefore, propose the hydrogenase from C. reinhardtii to be of the Fe‐only type. Adaptation in the presence of uncouplers of phosphorylation showed this process to be energy‐dependent. From protein synthesis inhibition experiments, it is concluded that the protein is synthesized on cytoplasmic ribosomes and, therefore, must be nuclear encoded. After isolation of intact chloroplasts from adapted cells, the active enzyme was shown, by Western‐blotting analysis, to be located in the chloroplasts.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8026490</pmid><doi>10.1111/j.1432-1033.1994.tb18923.x</doi><tpages>6</tpages></addata></record> |
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subjects | Adaptation, Physiological Anaerobiosis Animals Blotting, Western Chlamydomonas reinhardtii Chlamydomonas reinhardtii - enzymology Chlamydomonas reinhardtii - growth & development Chloramphenicol - pharmacology Chloroplasts - enzymology Cycloheximide - pharmacology Enzyme Induction - drug effects Freshwater Hydrogenase - analysis Hydrogenase - biosynthesis Hydrogenase - chemistry Iron - analysis Iron - pharmacology Nickel - pharmacology Phosphorylation Ribosomes - enzymology Spectrophotometry, Atomic Uncoupling Agents - pharmacology |
title | Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii |
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