Photosynthetic and other phosphoenolpyruvate carboxylase isoforms in the single-cell, facultative C(4) system of Hydrilla verticillata
The submersed monocot Hydrilla verticillata (L.f.) Royle is a facultative C(4) plant. It typically exhibits C(3) photosynthetic characteristics, but exposure to low [CO(2)] induces a C(4) system in which the C(4) and Calvin cycles co-exist in the same cell and the initial fixation in the light is ca...
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description | The submersed monocot Hydrilla verticillata (L.f.) Royle is a facultative C(4) plant. It typically exhibits C(3) photosynthetic characteristics, but exposure to low [CO(2)] induces a C(4) system in which the C(4) and Calvin cycles co-exist in the same cell and the initial fixation in the light is catalyzed by phosphoenolpyruvate carboxylase (PEPC). Three full-length cDNAs encoding PEPC were isolated from H. verticillata, two from leaves and one from root. The sequences were 95% to 99% identical and shared a 75% to 85% similarity with other plant PEPCs. Transcript studies revealed that one isoform, Hvpepc4, was exclusively expressed in leaves during C(4) induction. This and enzyme kinetic data were consistent with it being the C(4) photosynthesis isoform. However, the C(4) signature serine of terrestrial plant C(4) isoforms was absent in this and the other H. verticillata sequences. Instead, alanine, typical of C(3) sequences, was present. Western analyses of C(3) and C(4) leaf extracts after anion-exchange chromatography showed similar dominant PEPC-specific bands at 110 kD. In phylogenetic analyses, the sequences grouped with C(3), non-graminaceous C(4), and Crassulacean acid metabolism PEPCs but not with the graminaceous C(4), and formed a clade with a gymnosperm, which is consistent with H. verticillata PEPC predating that of other C(4) angiosperms. |
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Royle is a facultative C(4) plant. It typically exhibits C(3) photosynthetic characteristics, but exposure to low [CO(2)] induces a C(4) system in which the C(4) and Calvin cycles co-exist in the same cell and the initial fixation in the light is catalyzed by phosphoenolpyruvate carboxylase (PEPC). Three full-length cDNAs encoding PEPC were isolated from H. verticillata, two from leaves and one from root. The sequences were 95% to 99% identical and shared a 75% to 85% similarity with other plant PEPCs. Transcript studies revealed that one isoform, Hvpepc4, was exclusively expressed in leaves during C(4) induction. This and enzyme kinetic data were consistent with it being the C(4) photosynthesis isoform. However, the C(4) signature serine of terrestrial plant C(4) isoforms was absent in this and the other H. verticillata sequences. Instead, alanine, typical of C(3) sequences, was present. Western analyses of C(3) and C(4) leaf extracts after anion-exchange chromatography showed similar dominant PEPC-specific bands at 110 kD. In phylogenetic analyses, the sequences grouped with C(3), non-graminaceous C(4), and Crassulacean acid metabolism PEPCs but not with the graminaceous C(4), and formed a clade with a gymnosperm, which is consistent with H. verticillata PEPC predating that of other C(4) angiosperms.</description><identifier>ISSN: 0032-0889</identifier><identifier>DOI: 10.1104/pp.008045</identifier><identifier>PMID: 12376652</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Blotting, Western ; Cloning, Molecular ; DNA, Complementary ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Plant ; Hydrocharitaceae - cytology ; Hydrocharitaceae - enzymology ; Hydrocharitaceae - genetics ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Kinetics ; Molecular Sequence Data ; Phosphoenolpyruvate Carboxylase - genetics ; Phosphoenolpyruvate Carboxylase - isolation & purification ; Phosphoenolpyruvate Carboxylase - metabolism ; Photosynthesis - physiology ; Photosynthetic Reaction Center Complex Proteins - classification ; Photosynthetic Reaction Center Complex Proteins - metabolism ; Phylogeny ; Plant Leaves - enzymology ; Plant Leaves - genetics ; Plant Roots - enzymology ; Plant Roots - genetics</subject><ispartof>Plant physiology (Bethesda), 2002-10, Vol.130 (2), p.876</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12376652$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rao, Srinath K</creatorcontrib><creatorcontrib>Magnin, Noël C</creatorcontrib><creatorcontrib>Reiskind, Julia B</creatorcontrib><creatorcontrib>Bowes, George</creatorcontrib><title>Photosynthetic and other phosphoenolpyruvate carboxylase isoforms in the single-cell, facultative C(4) system of Hydrilla verticillata</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The submersed monocot Hydrilla verticillata (L.f.) Royle is a facultative C(4) plant. It typically exhibits C(3) photosynthetic characteristics, but exposure to low [CO(2)] induces a C(4) system in which the C(4) and Calvin cycles co-exist in the same cell and the initial fixation in the light is catalyzed by phosphoenolpyruvate carboxylase (PEPC). Three full-length cDNAs encoding PEPC were isolated from H. verticillata, two from leaves and one from root. The sequences were 95% to 99% identical and shared a 75% to 85% similarity with other plant PEPCs. Transcript studies revealed that one isoform, Hvpepc4, was exclusively expressed in leaves during C(4) induction. This and enzyme kinetic data were consistent with it being the C(4) photosynthesis isoform. However, the C(4) signature serine of terrestrial plant C(4) isoforms was absent in this and the other H. verticillata sequences. Instead, alanine, typical of C(3) sequences, was present. Western analyses of C(3) and C(4) leaf extracts after anion-exchange chromatography showed similar dominant PEPC-specific bands at 110 kD. In phylogenetic analyses, the sequences grouped with C(3), non-graminaceous C(4), and Crassulacean acid metabolism PEPCs but not with the graminaceous C(4), and formed a clade with a gymnosperm, which is consistent with H. verticillata PEPC predating that of other C(4) angiosperms.</description><subject>Amino Acid Sequence</subject><subject>Blotting, Western</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Gene Expression Regulation, Plant</subject><subject>Hydrocharitaceae - cytology</subject><subject>Hydrocharitaceae - enzymology</subject><subject>Hydrocharitaceae - genetics</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Phosphoenolpyruvate Carboxylase - genetics</subject><subject>Phosphoenolpyruvate Carboxylase - isolation & purification</subject><subject>Phosphoenolpyruvate Carboxylase - metabolism</subject><subject>Photosynthesis - physiology</subject><subject>Photosynthetic Reaction Center Complex Proteins - classification</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>Phylogeny</subject><subject>Plant Leaves - enzymology</subject><subject>Plant Leaves - genetics</subject><subject>Plant Roots - enzymology</subject><subject>Plant Roots - genetics</subject><issn>0032-0889</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kMFOwzAQRH0A0VI48APIJwQSKWs7iZ0jqoAiVYJD75GT2NTIiYPtVOQH-G5SUQ6rncOb3dEgdEVgSQikD32_BBCQZidoDsBoAkIUM3QewicAEEbSMzQjlPE8z-gc_bzvXHRh7OJORVNj2TXYTdrjfufCNKpzth_9sJdR4Vr6yn2PVgaFTXDa-TZg0-HJgIPpPqxKamXtPdayHmyU0ewVXt2mdziMIaoWO43XY-ONtRLvlZ8-HmSUF-hUSxvU5XEv0Pb5abtaJ5u3l9fV4ybps5Qmqmkq4DontWQUCsZTURQctNC5zCpREZJWIDhlglRMCEkz3uQNZxyoynnG2QLd_J3tvfsaVIhla8IhseyUG0LJKcmLqaIJvD6CQ9Wqpuy9aaUfy__i2C9tQW7l</recordid><startdate>200210</startdate><enddate>200210</enddate><creator>Rao, Srinath K</creator><creator>Magnin, Noël C</creator><creator>Reiskind, Julia B</creator><creator>Bowes, George</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200210</creationdate><title>Photosynthetic and other phosphoenolpyruvate carboxylase isoforms in the single-cell, facultative C(4) system of Hydrilla verticillata</title><author>Rao, Srinath K ; Magnin, Noël C ; Reiskind, Julia B ; Bowes, George</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p542-eddb07f61ca320937489970f8f6a5b8b114b0872381b388a257d6d73702e67573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Blotting, Western</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Gene Expression Regulation, Plant</topic><topic>Hydrocharitaceae - cytology</topic><topic>Hydrocharitaceae - enzymology</topic><topic>Hydrocharitaceae - genetics</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Phosphoenolpyruvate Carboxylase - genetics</topic><topic>Phosphoenolpyruvate Carboxylase - isolation & purification</topic><topic>Phosphoenolpyruvate Carboxylase - metabolism</topic><topic>Photosynthesis - physiology</topic><topic>Photosynthetic Reaction Center Complex Proteins - classification</topic><topic>Photosynthetic Reaction Center Complex Proteins - metabolism</topic><topic>Phylogeny</topic><topic>Plant Leaves - enzymology</topic><topic>Plant Leaves - genetics</topic><topic>Plant Roots - enzymology</topic><topic>Plant Roots - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rao, Srinath K</creatorcontrib><creatorcontrib>Magnin, Noël C</creatorcontrib><creatorcontrib>Reiskind, Julia B</creatorcontrib><creatorcontrib>Bowes, George</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rao, Srinath K</au><au>Magnin, Noël C</au><au>Reiskind, Julia B</au><au>Bowes, George</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Photosynthetic and other phosphoenolpyruvate carboxylase isoforms in the single-cell, facultative C(4) system of Hydrilla verticillata</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2002-10</date><risdate>2002</risdate><volume>130</volume><issue>2</issue><spage>876</spage><pages>876-</pages><issn>0032-0889</issn><abstract>The submersed monocot Hydrilla verticillata (L.f.) Royle is a facultative C(4) plant. It typically exhibits C(3) photosynthetic characteristics, but exposure to low [CO(2)] induces a C(4) system in which the C(4) and Calvin cycles co-exist in the same cell and the initial fixation in the light is catalyzed by phosphoenolpyruvate carboxylase (PEPC). Three full-length cDNAs encoding PEPC were isolated from H. verticillata, two from leaves and one from root. The sequences were 95% to 99% identical and shared a 75% to 85% similarity with other plant PEPCs. Transcript studies revealed that one isoform, Hvpepc4, was exclusively expressed in leaves during C(4) induction. This and enzyme kinetic data were consistent with it being the C(4) photosynthesis isoform. However, the C(4) signature serine of terrestrial plant C(4) isoforms was absent in this and the other H. verticillata sequences. Instead, alanine, typical of C(3) sequences, was present. Western analyses of C(3) and C(4) leaf extracts after anion-exchange chromatography showed similar dominant PEPC-specific bands at 110 kD. In phylogenetic analyses, the sequences grouped with C(3), non-graminaceous C(4), and Crassulacean acid metabolism PEPCs but not with the graminaceous C(4), and formed a clade with a gymnosperm, which is consistent with H. verticillata PEPC predating that of other C(4) angiosperms.</abstract><cop>United States</cop><pmid>12376652</pmid><doi>10.1104/pp.008045</doi></addata></record> |
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source | MEDLINE; JSTOR Archive Collection A-Z Listing; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
subjects | Amino Acid Sequence Blotting, Western Cloning, Molecular DNA, Complementary Gene Expression Regulation, Enzymologic Gene Expression Regulation, Plant Hydrocharitaceae - cytology Hydrocharitaceae - enzymology Hydrocharitaceae - genetics Isoenzymes - genetics Isoenzymes - metabolism Kinetics Molecular Sequence Data Phosphoenolpyruvate Carboxylase - genetics Phosphoenolpyruvate Carboxylase - isolation & purification Phosphoenolpyruvate Carboxylase - metabolism Photosynthesis - physiology Photosynthetic Reaction Center Complex Proteins - classification Photosynthetic Reaction Center Complex Proteins - metabolism Phylogeny Plant Leaves - enzymology Plant Leaves - genetics Plant Roots - enzymology Plant Roots - genetics |
title | Photosynthetic and other phosphoenolpyruvate carboxylase isoforms in the single-cell, facultative C(4) system of Hydrilla verticillata |
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