A Novel Phosphatidylcholine-hydrolyzing Phospholipase C Induced by Phosphate Starvation in Arabidopsis
During phosphate starvation, it is known that phospholipids are degraded, and conversely, a nonphosphorus galactolipid digalactosyldiacylglycerol accumulates in the root plasma membrane of plants. We report a novel phospholipase C that hydrolyzes phosphatidylcholine and is greatly induced in respons...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-03, Vol.280 (9), p.7469-7476 |
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| creator | Nakamura, Yuki Awai, Koichiro Masuda, Tatsuru Yoshioka, Yasushi Takamiya, Ken-ichiro Ohta, Hiroyuki |
| description | During phosphate starvation, it is known that phospholipids are degraded, and conversely, a nonphosphorus galactolipid digalactosyldiacylglycerol
accumulates in the root plasma membrane of plants. We report a novel phospholipase C that hydrolyzes phosphatidylcholine and
is greatly induced in response to phosphate deprivation in Arabidopsis . Since phosphatidylcholine-hydrolyzing activity by phospholipase C was highly up-regulated in phosphate-deprived plants,
gene expression of some phospholipase C was expected to be induced during phosphate starvation. Based on amino acid sequence
similarity to a bacterial phosphatidylcholine-hydrolyzing phospholipase C, six putative phospholipase Cs were identified in
the Arabidopsis genome, one of which, NPC4 , showed significant transcriptional activation upon phosphate limitation. Molecular cloning and functional expression of
NPC4 confirmed that the NPC4 gene encoded a functional phosphatidylcholine-hydrolyzing phospholipase C that did not require Ca 2+ for its activity. Subcellular localization analysis showed that NPC4 protein was highly enriched in the plasma membrane.
Analyses of transferred DNA-tagged npc4 mutants revealed that disruption of NPC4 severely reduces the phosphatidylcholine-hydrolyzing phospholipase C activity in response to phosphate starvation. These
results suggest that NPC4 plays an important role in the supply of both inorganic phosphate and diacylglycerol from membrane-localized
phospholipids that would be used for phosphate supplementation and the replacement of polar lipids in the root plasma membrane
during phosphate deprivation. |
| doi_str_mv | 10.1074/jbc.M408799200 |
| format | Article |
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accumulates in the root plasma membrane of plants. We report a novel phospholipase C that hydrolyzes phosphatidylcholine and
is greatly induced in response to phosphate deprivation in Arabidopsis . Since phosphatidylcholine-hydrolyzing activity by phospholipase C was highly up-regulated in phosphate-deprived plants,
gene expression of some phospholipase C was expected to be induced during phosphate starvation. Based on amino acid sequence
similarity to a bacterial phosphatidylcholine-hydrolyzing phospholipase C, six putative phospholipase Cs were identified in
the Arabidopsis genome, one of which, NPC4 , showed significant transcriptional activation upon phosphate limitation. Molecular cloning and functional expression of
NPC4 confirmed that the NPC4 gene encoded a functional phosphatidylcholine-hydrolyzing phospholipase C that did not require Ca 2+ for its activity. Subcellular localization analysis showed that NPC4 protein was highly enriched in the plasma membrane.
Analyses of transferred DNA-tagged npc4 mutants revealed that disruption of NPC4 severely reduces the phosphatidylcholine-hydrolyzing phospholipase C activity in response to phosphate starvation. These
results suggest that NPC4 plays an important role in the supply of both inorganic phosphate and diacylglycerol from membrane-localized
phospholipids that would be used for phosphate supplementation and the replacement of polar lipids in the root plasma membrane
during phosphate deprivation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M408799200</identifier><identifier>PMID: 15618226</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis Proteins - biosynthesis ; Arabidopsis Proteins - physiology ; Bacterial Proteins - chemistry ; Blotting, Northern ; Blotting, Western ; Calcium - metabolism ; Cell Membrane - metabolism ; Chloroplasts - metabolism ; Chromatography, Thin Layer ; Cloning, Molecular ; DNA - chemistry ; Dose-Response Relationship, Drug ; Escherichia coli - metabolism ; Genes, Plant ; Genome, Plant ; Hydrolysis ; Lipid Metabolism ; Models, Biological ; Models, Genetic ; Molecular Sequence Data ; Phosphates - chemistry ; Phosphates - metabolism ; Phosphatidylcholines - chemistry ; Phospholipids - metabolism ; Plant Proteins - biosynthesis ; Plant Roots - metabolism ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Transcriptional Activation ; Type C Phospholipases - biosynthesis ; Type C Phospholipases - chemistry ; Type C Phospholipases - metabolism ; Type C Phospholipases - physiology ; Up-Regulation</subject><ispartof>The Journal of biological chemistry, 2005-03, Vol.280 (9), p.7469-7476</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c436t-9d6c5c83d50d70a27b25f83acef502872b6203f1e1cfebf2ca2a1b61a860b13a3</citedby><cites>FETCH-LOGICAL-c436t-9d6c5c83d50d70a27b25f83acef502872b6203f1e1cfebf2ca2a1b61a860b13a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15618226$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakamura, Yuki</creatorcontrib><creatorcontrib>Awai, Koichiro</creatorcontrib><creatorcontrib>Masuda, Tatsuru</creatorcontrib><creatorcontrib>Yoshioka, Yasushi</creatorcontrib><creatorcontrib>Takamiya, Ken-ichiro</creatorcontrib><creatorcontrib>Ohta, Hiroyuki</creatorcontrib><title>A Novel Phosphatidylcholine-hydrolyzing Phospholipase C Induced by Phosphate Starvation in Arabidopsis</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>During phosphate starvation, it is known that phospholipids are degraded, and conversely, a nonphosphorus galactolipid digalactosyldiacylglycerol
accumulates in the root plasma membrane of plants. We report a novel phospholipase C that hydrolyzes phosphatidylcholine and
is greatly induced in response to phosphate deprivation in Arabidopsis . Since phosphatidylcholine-hydrolyzing activity by phospholipase C was highly up-regulated in phosphate-deprived plants,
gene expression of some phospholipase C was expected to be induced during phosphate starvation. Based on amino acid sequence
similarity to a bacterial phosphatidylcholine-hydrolyzing phospholipase C, six putative phospholipase Cs were identified in
the Arabidopsis genome, one of which, NPC4 , showed significant transcriptional activation upon phosphate limitation. Molecular cloning and functional expression of
NPC4 confirmed that the NPC4 gene encoded a functional phosphatidylcholine-hydrolyzing phospholipase C that did not require Ca 2+ for its activity. Subcellular localization analysis showed that NPC4 protein was highly enriched in the plasma membrane.
Analyses of transferred DNA-tagged npc4 mutants revealed that disruption of NPC4 severely reduces the phosphatidylcholine-hydrolyzing phospholipase C activity in response to phosphate starvation. These
results suggest that NPC4 plays an important role in the supply of both inorganic phosphate and diacylglycerol from membrane-localized
phospholipids that would be used for phosphate supplementation and the replacement of polar lipids in the root plasma membrane
during phosphate deprivation.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis Proteins - biosynthesis</subject><subject>Arabidopsis Proteins - physiology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>Calcium - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Chloroplasts - metabolism</subject><subject>Chromatography, Thin Layer</subject><subject>Cloning, Molecular</subject><subject>DNA - chemistry</subject><subject>Dose-Response Relationship, Drug</subject><subject>Escherichia coli - metabolism</subject><subject>Genes, Plant</subject><subject>Genome, Plant</subject><subject>Hydrolysis</subject><subject>Lipid Metabolism</subject><subject>Models, Biological</subject><subject>Models, Genetic</subject><subject>Molecular Sequence Data</subject><subject>Phosphates - chemistry</subject><subject>Phosphates - metabolism</subject><subject>Phosphatidylcholines - chemistry</subject><subject>Phospholipids - metabolism</subject><subject>Plant Proteins - biosynthesis</subject><subject>Plant Roots - metabolism</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transcriptional Activation</subject><subject>Type C Phospholipases - biosynthesis</subject><subject>Type C Phospholipases - chemistry</subject><subject>Type C Phospholipases - metabolism</subject><subject>Type C Phospholipases - physiology</subject><subject>Up-Regulation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkEtLw0AURgdRbK1uXUpw4S51HnlMlqX4KNQHqOBumFeaKUkmziSV-OuNNNi7uXDv-b7FAeASwTmCaXS7FXL-FEGaZhmG8AhMEaQkJDH6PAZTCDEKMxzTCTjzfguHiTJ0CiYoThDFOJmCfBE8250ug9fC-qbgrVF9KQtbmlqHRa-cLfsfU2_G_3BvuNfBMljVqpNaBaL_j-rgreVuN3TYOjB1sHBcGGUbb_w5OMl56fXFuGfg4_7uffkYrl8eVsvFOpQRSdowU4mMJSUqhiqFHKcCxzklXOo8hpimWCQYkhxpJHMtciw55kgkiNMECkQ4mYGbfW_j7Fenfcsq46UuS15r23mGUopwFKUDON-D0lnvnc5Z40zFXc8QZH9m2WCWHcwOgauxuROVVgd8VDkA13ugMJvi2zjNhLGy0BXDFLKMpVGSkV9azIHI</recordid><startdate>20050304</startdate><enddate>20050304</enddate><creator>Nakamura, Yuki</creator><creator>Awai, Koichiro</creator><creator>Masuda, Tatsuru</creator><creator>Yoshioka, Yasushi</creator><creator>Takamiya, Ken-ichiro</creator><creator>Ohta, Hiroyuki</creator><general>American Society for Biochemistry and Molecular Biology</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>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20050304</creationdate><title>A Novel Phosphatidylcholine-hydrolyzing Phospholipase C Induced by Phosphate Starvation in Arabidopsis</title><author>Nakamura, Yuki ; Awai, Koichiro ; Masuda, Tatsuru ; Yoshioka, Yasushi ; Takamiya, Ken-ichiro ; Ohta, Hiroyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c436t-9d6c5c83d50d70a27b25f83acef502872b6203f1e1cfebf2ca2a1b61a860b13a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis Proteins - biosynthesis</topic><topic>Arabidopsis Proteins - physiology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Blotting, Northern</topic><topic>Blotting, Western</topic><topic>Calcium - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Chloroplasts - metabolism</topic><topic>Chromatography, Thin Layer</topic><topic>Cloning, Molecular</topic><topic>DNA - chemistry</topic><topic>Dose-Response Relationship, Drug</topic><topic>Escherichia coli - metabolism</topic><topic>Genes, Plant</topic><topic>Genome, Plant</topic><topic>Hydrolysis</topic><topic>Lipid Metabolism</topic><topic>Models, Biological</topic><topic>Models, Genetic</topic><topic>Molecular Sequence Data</topic><topic>Phosphates - chemistry</topic><topic>Phosphates - metabolism</topic><topic>Phosphatidylcholines - chemistry</topic><topic>Phospholipids - metabolism</topic><topic>Plant Proteins - biosynthesis</topic><topic>Plant Roots - metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transcriptional Activation</topic><topic>Type C Phospholipases - biosynthesis</topic><topic>Type C Phospholipases - chemistry</topic><topic>Type C Phospholipases - metabolism</topic><topic>Type C Phospholipases - physiology</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakamura, Yuki</creatorcontrib><creatorcontrib>Awai, Koichiro</creatorcontrib><creatorcontrib>Masuda, Tatsuru</creatorcontrib><creatorcontrib>Yoshioka, Yasushi</creatorcontrib><creatorcontrib>Takamiya, Ken-ichiro</creatorcontrib><creatorcontrib>Ohta, Hiroyuki</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>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakamura, Yuki</au><au>Awai, Koichiro</au><au>Masuda, Tatsuru</au><au>Yoshioka, Yasushi</au><au>Takamiya, Ken-ichiro</au><au>Ohta, Hiroyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Novel Phosphatidylcholine-hydrolyzing Phospholipase C Induced by Phosphate Starvation in Arabidopsis</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-03-04</date><risdate>2005</risdate><volume>280</volume><issue>9</issue><spage>7469</spage><epage>7476</epage><pages>7469-7476</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>During phosphate starvation, it is known that phospholipids are degraded, and conversely, a nonphosphorus galactolipid digalactosyldiacylglycerol
accumulates in the root plasma membrane of plants. We report a novel phospholipase C that hydrolyzes phosphatidylcholine and
is greatly induced in response to phosphate deprivation in Arabidopsis . Since phosphatidylcholine-hydrolyzing activity by phospholipase C was highly up-regulated in phosphate-deprived plants,
gene expression of some phospholipase C was expected to be induced during phosphate starvation. Based on amino acid sequence
similarity to a bacterial phosphatidylcholine-hydrolyzing phospholipase C, six putative phospholipase Cs were identified in
the Arabidopsis genome, one of which, NPC4 , showed significant transcriptional activation upon phosphate limitation. Molecular cloning and functional expression of
NPC4 confirmed that the NPC4 gene encoded a functional phosphatidylcholine-hydrolyzing phospholipase C that did not require Ca 2+ for its activity. Subcellular localization analysis showed that NPC4 protein was highly enriched in the plasma membrane.
Analyses of transferred DNA-tagged npc4 mutants revealed that disruption of NPC4 severely reduces the phosphatidylcholine-hydrolyzing phospholipase C activity in response to phosphate starvation. These
results suggest that NPC4 plays an important role in the supply of both inorganic phosphate and diacylglycerol from membrane-localized
phospholipids that would be used for phosphate supplementation and the replacement of polar lipids in the root plasma membrane
during phosphate deprivation.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15618226</pmid><doi>10.1074/jbc.M408799200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Arabidopsis Arabidopsis - enzymology Arabidopsis Proteins - biosynthesis Arabidopsis Proteins - physiology Bacterial Proteins - chemistry Blotting, Northern Blotting, Western Calcium - metabolism Cell Membrane - metabolism Chloroplasts - metabolism Chromatography, Thin Layer Cloning, Molecular DNA - chemistry Dose-Response Relationship, Drug Escherichia coli - metabolism Genes, Plant Genome, Plant Hydrolysis Lipid Metabolism Models, Biological Models, Genetic Molecular Sequence Data Phosphates - chemistry Phosphates - metabolism Phosphatidylcholines - chemistry Phospholipids - metabolism Plant Proteins - biosynthesis Plant Roots - metabolism Protein Structure, Tertiary Sequence Homology, Amino Acid Transcriptional Activation Type C Phospholipases - biosynthesis Type C Phospholipases - chemistry Type C Phospholipases - metabolism Type C Phospholipases - physiology Up-Regulation |
| title | A Novel Phosphatidylcholine-hydrolyzing Phospholipase C Induced by Phosphate Starvation in Arabidopsis |
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