Cloning and characterization of a plastidic glycerol 3-phosphate dehydrogenase cDNA from Dunaliella salina
A cDNA encoding a nicotinamide adenine dinucleotide (NAD +)-dependent glycerol 3-phosphate dehydrogenase (GPDH) has been cloned by rapid amplification of cDNA ends from Dunaliella salina. The cDNA is 3032 base pairs long with an open reading frame encoding a polypeptide of 701 amino acids. The polyp...
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| Veröffentlicht in: | Journal of plant physiology 2007-02, Vol.164 (2), p.214-220 |
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| creator | He, Qinghua Qiao, Dairong Bai, Linhan Zhang, Qinglian Yang, Wanggui Li, Qian Cao, Yi |
| description | A cDNA encoding a nicotinamide adenine dinucleotide (NAD
+)-dependent glycerol 3-phosphate dehydrogenase (GPDH) has been cloned by rapid amplification of cDNA ends from
Dunaliella salina. The cDNA is 3032 base pairs long with an open reading frame encoding a polypeptide of 701 amino acids. The polypeptide shows high homology with published NAD
+-dependent GPDHs and has at its N-terminal a chloroplast targeting sequence. RNA gel blot analysis was performed to study GPDH gene expression under different conditions, and changes of the glycerol content were monitored. The results indicate that the cDNA may encode an osmoregulated isoform primarily involved in glycerol synthesis. The 701-amino-acid polypeptide is about 300 amino acids longer than previously reported plant NAD
+-dependent GPDHs. This 300-amino-acid fragment has a phosphoserine phosphatase domain. We suggest that the phosphoserine phosphatase domain functions as glycerol 3-phosphatase and that, consequently, NAD
+-dependent GPDH from
D. salina can catalyze the step from dihydroxyacetone phosphate to glycerol directly. This is unique and a possible explanation for the fast glycerol synthesis found in
D. salina. |
| doi_str_mv | 10.1016/j.jplph.2006.04.004 |
| format | Article |
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+)-dependent glycerol 3-phosphate dehydrogenase (GPDH) has been cloned by rapid amplification of cDNA ends from
Dunaliella salina. The cDNA is 3032 base pairs long with an open reading frame encoding a polypeptide of 701 amino acids. The polypeptide shows high homology with published NAD
+-dependent GPDHs and has at its N-terminal a chloroplast targeting sequence. RNA gel blot analysis was performed to study GPDH gene expression under different conditions, and changes of the glycerol content were monitored. The results indicate that the cDNA may encode an osmoregulated isoform primarily involved in glycerol synthesis. The 701-amino-acid polypeptide is about 300 amino acids longer than previously reported plant NAD
+-dependent GPDHs. This 300-amino-acid fragment has a phosphoserine phosphatase domain. We suggest that the phosphoserine phosphatase domain functions as glycerol 3-phosphatase and that, consequently, NAD
+-dependent GPDH from
D. salina can catalyze the step from dihydroxyacetone phosphate to glycerol directly. This is unique and a possible explanation for the fast glycerol synthesis found in
D. salina.</description><identifier>ISSN: 0176-1617</identifier><identifier>EISSN: 1618-1328</identifier><identifier>DOI: 10.1016/j.jplph.2006.04.004</identifier><identifier>PMID: 16769151</identifier><identifier>CODEN: JPPHEY</identifier><language>eng</language><publisher>Jena: Elsevier GmbH</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; Chlorophyta - enzymology ; Chlorophyta - genetics ; Chlorophyta - metabolism ; Dunaliella salina ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Glycerol ; Glycerol - metabolism ; Glycerol 3-phosphatase ; Glycerol 3-phosphate dehydrogenase ; Glycerolphosphate Dehydrogenase - genetics ; Glycerolphosphate Dehydrogenase - metabolism ; Metabolism ; Molecular Sequence Data ; Osmotic stress ; Plant physiology and development ; Plastids - metabolism ; Sequence Analysis, DNA</subject><ispartof>Journal of plant physiology, 2007-02, Vol.164 (2), p.214-220</ispartof><rights>2006 Elsevier GmbH</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-2850347a17254fe6d5dd37b90bbb911e263b567988f4d90061d8cc310ba359213</citedby><cites>FETCH-LOGICAL-c418t-2850347a17254fe6d5dd37b90bbb911e263b567988f4d90061d8cc310ba359213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0176161706001337$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18893013$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16769151$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>He, Qinghua</creatorcontrib><creatorcontrib>Qiao, Dairong</creatorcontrib><creatorcontrib>Bai, Linhan</creatorcontrib><creatorcontrib>Zhang, Qinglian</creatorcontrib><creatorcontrib>Yang, Wanggui</creatorcontrib><creatorcontrib>Li, Qian</creatorcontrib><creatorcontrib>Cao, Yi</creatorcontrib><title>Cloning and characterization of a plastidic glycerol 3-phosphate dehydrogenase cDNA from Dunaliella salina</title><title>Journal of plant physiology</title><addtitle>J Plant Physiol</addtitle><description>A cDNA encoding a nicotinamide adenine dinucleotide (NAD
+)-dependent glycerol 3-phosphate dehydrogenase (GPDH) has been cloned by rapid amplification of cDNA ends from
Dunaliella salina. The cDNA is 3032 base pairs long with an open reading frame encoding a polypeptide of 701 amino acids. The polypeptide shows high homology with published NAD
+-dependent GPDHs and has at its N-terminal a chloroplast targeting sequence. RNA gel blot analysis was performed to study GPDH gene expression under different conditions, and changes of the glycerol content were monitored. The results indicate that the cDNA may encode an osmoregulated isoform primarily involved in glycerol synthesis. The 701-amino-acid polypeptide is about 300 amino acids longer than previously reported plant NAD
+-dependent GPDHs. This 300-amino-acid fragment has a phosphoserine phosphatase domain. We suggest that the phosphoserine phosphatase domain functions as glycerol 3-phosphatase and that, consequently, NAD
+-dependent GPDH from
D. salina can catalyze the step from dihydroxyacetone phosphate to glycerol directly. This is unique and a possible explanation for the fast glycerol synthesis found in
D. salina.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Chlorophyta - enzymology</subject><subject>Chlorophyta - genetics</subject><subject>Chlorophyta - metabolism</subject><subject>Dunaliella salina</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Glycerol</subject><subject>Glycerol - metabolism</subject><subject>Glycerol 3-phosphatase</subject><subject>Glycerol 3-phosphate dehydrogenase</subject><subject>Glycerolphosphate Dehydrogenase - genetics</subject><subject>Glycerolphosphate Dehydrogenase - metabolism</subject><subject>Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Osmotic stress</subject><subject>Plant physiology and development</subject><subject>Plastids - metabolism</subject><subject>Sequence Analysis, DNA</subject><issn>0176-1617</issn><issn>1618-1328</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EokvhFyAhX-CW4IkTxzlwqLZQkCq4wNly7MnGkdcOdhZp-fVkuyv1Vk7zoWdezcxLyFtgJTAQH6dymv08lhVjomR1yVj9jGxAgCyAV_I52TBoRbE22ivyKueJrXUj-UtyBaIVHTSwIdPWx-DCjupgqRl10mbB5P7qxcVA40A1nb3Oi7PO0J0_GkzRU17MY8zzqBekFsejTXGHQWek5vb7DR1S3NPbQ9Deofea5jUJ-jV5MWif8c0lXpNfXz7_3H4t7n_cfdve3BemBrkUlWwYr1sNbdXUAwrbWMvbvmN933cAWAneN6LtpBxq2623g5XGcGC95k1XAb8mH866c4q_D5gXtXfZnBYJGA9ZtawSomP1f0HoRLPqiRXkZ9CkmHPCQc3J7XU6KmDq5IWa1IMX6uSFYrViD_LvLvKHfo_2ceby_BV4fwF0NtoPSQfj8iMnZccZ8JX7dOZw_dofh0ll4zAYtC6hWZSN7slF_gEqW6g5</recordid><startdate>20070201</startdate><enddate>20070201</enddate><creator>He, Qinghua</creator><creator>Qiao, Dairong</creator><creator>Bai, Linhan</creator><creator>Zhang, Qinglian</creator><creator>Yang, Wanggui</creator><creator>Li, Qian</creator><creator>Cao, Yi</creator><general>Elsevier GmbH</general><general>Elsevier</general><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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20070201</creationdate><title>Cloning and characterization of a plastidic glycerol 3-phosphate dehydrogenase cDNA from Dunaliella salina</title><author>He, Qinghua ; Qiao, Dairong ; Bai, Linhan ; Zhang, Qinglian ; Yang, Wanggui ; Li, Qian ; Cao, Yi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-2850347a17254fe6d5dd37b90bbb911e263b567988f4d90061d8cc310ba359213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Chlorophyta - enzymology</topic><topic>Chlorophyta - genetics</topic><topic>Chlorophyta - metabolism</topic><topic>Dunaliella salina</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Glycerol</topic><topic>Glycerol - metabolism</topic><topic>Glycerol 3-phosphatase</topic><topic>Glycerol 3-phosphate dehydrogenase</topic><topic>Glycerolphosphate Dehydrogenase - genetics</topic><topic>Glycerolphosphate Dehydrogenase - metabolism</topic><topic>Metabolism</topic><topic>Molecular Sequence Data</topic><topic>Osmotic stress</topic><topic>Plant physiology and development</topic><topic>Plastids - metabolism</topic><topic>Sequence Analysis, DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>He, Qinghua</creatorcontrib><creatorcontrib>Qiao, Dairong</creatorcontrib><creatorcontrib>Bai, Linhan</creatorcontrib><creatorcontrib>Zhang, Qinglian</creatorcontrib><creatorcontrib>Yang, Wanggui</creatorcontrib><creatorcontrib>Li, Qian</creatorcontrib><creatorcontrib>Cao, Yi</creatorcontrib><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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of plant physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>He, Qinghua</au><au>Qiao, Dairong</au><au>Bai, Linhan</au><au>Zhang, Qinglian</au><au>Yang, Wanggui</au><au>Li, Qian</au><au>Cao, Yi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and characterization of a plastidic glycerol 3-phosphate dehydrogenase cDNA from Dunaliella salina</atitle><jtitle>Journal of plant physiology</jtitle><addtitle>J Plant Physiol</addtitle><date>2007-02-01</date><risdate>2007</risdate><volume>164</volume><issue>2</issue><spage>214</spage><epage>220</epage><pages>214-220</pages><issn>0176-1617</issn><eissn>1618-1328</eissn><coden>JPPHEY</coden><abstract>A cDNA encoding a nicotinamide adenine dinucleotide (NAD
+)-dependent glycerol 3-phosphate dehydrogenase (GPDH) has been cloned by rapid amplification of cDNA ends from
Dunaliella salina. The cDNA is 3032 base pairs long with an open reading frame encoding a polypeptide of 701 amino acids. The polypeptide shows high homology with published NAD
+-dependent GPDHs and has at its N-terminal a chloroplast targeting sequence. RNA gel blot analysis was performed to study GPDH gene expression under different conditions, and changes of the glycerol content were monitored. The results indicate that the cDNA may encode an osmoregulated isoform primarily involved in glycerol synthesis. The 701-amino-acid polypeptide is about 300 amino acids longer than previously reported plant NAD
+-dependent GPDHs. This 300-amino-acid fragment has a phosphoserine phosphatase domain. We suggest that the phosphoserine phosphatase domain functions as glycerol 3-phosphatase and that, consequently, NAD
+-dependent GPDH from
D. salina can catalyze the step from dihydroxyacetone phosphate to glycerol directly. This is unique and a possible explanation for the fast glycerol synthesis found in
D. salina.</abstract><cop>Jena</cop><pub>Elsevier GmbH</pub><pmid>16769151</pmid><doi>10.1016/j.jplph.2006.04.004</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Biological and medical sciences Chlorophyta - enzymology Chlorophyta - genetics Chlorophyta - metabolism Dunaliella salina Enzymes Fundamental and applied biological sciences. Psychology Gene Expression Glycerol Glycerol - metabolism Glycerol 3-phosphatase Glycerol 3-phosphate dehydrogenase Glycerolphosphate Dehydrogenase - genetics Glycerolphosphate Dehydrogenase - metabolism Metabolism Molecular Sequence Data Osmotic stress Plant physiology and development Plastids - metabolism Sequence Analysis, DNA |
| title | Cloning and characterization of a plastidic glycerol 3-phosphate dehydrogenase cDNA from Dunaliella salina |
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