New Insights Into Sunflower (Helianthus annuus L.) FatA and FatB Thioesterases, Their Regulation, Structure and Distribution
Sunflower seeds ( L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity , the enzymes that terminate the process of fatty acid synthesis by catalyzing the hydrol...
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| Published in | Frontiers in plant science Vol. 9; p. 1496 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Frontiers Media S.A
16.10.2018
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| Online Access | Get full text |
| ISSN | 1664-462X 1664-462X |
| DOI | 10.3389/fpls.2018.01496 |
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| Abstract | Sunflower seeds (
L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity
, the enzymes that terminate the process of
fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using
imaging and organelle fractionation,
thioesterases,
FatA and
FatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by
FatA and
FatB in oil biosynthesis are discussed in the light of our data. |
|---|---|
| AbstractList | Sunflower seeds (
L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity
, the enzymes that terminate the process of
fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using
imaging and organelle fractionation,
thioesterases,
FatA and
FatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by
FatA and
FatB in oil biosynthesis are discussed in the light of our data. Sunflower seeds ( Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity in vitro , the enzymes that terminate the process of de novo fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using in vivo imaging and organelle fractionation, H. annuus thioesterases, Ha FatA and Ha FatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by Ha FatA and Ha FatB in oil biosynthesis are discussed in the light of our data. Sunflower seeds (Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity in vitro, the enzymes that terminate the process of de novo fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using in vivo imaging and organelle fractionation, H. annuus thioesterases, HaFatA and HaFatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by HaFatA and HaFatB in oil biosynthesis are discussed in the light of our data. Sunflower seeds (Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity in vitro, the enzymes that terminate the process of de novo fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using in vivo imaging and organelle fractionation, H. annuus thioesterases, HaFatA and HaFatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by HaFatA and HaFatB in oil biosynthesis are discussed in the light of our data.Sunflower seeds (Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity in vitro, the enzymes that terminate the process of de novo fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using in vivo imaging and organelle fractionation, H. annuus thioesterases, HaFatA and HaFatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by HaFatA and HaFatB in oil biosynthesis are discussed in the light of our data. |
| Author | Garcés, Rafael Aznar-Moreno, Jose A. Moreno-Pérez, Antonio J. Venegas Calerón, Mónica Gidda, Satinder K. Sánchez, Rosario Salas, Joaquín J. Martínez-Force, Enrique Mullen, Robert T. |
| AuthorAffiliation | 1 Department of Biochemistry and Molecular Biophysics, Kansas State University , Manhattan, KS , United States 4 Departamento de Genética, Facultad de Biología, Universidad de Sevilla , Seville , Spain 3 Department of Molecular and Cellular Biology, University of Guelph , Guelph, ON , Canada 2 Instituto de la Grasa (CSIC), Campus Universitario Pablo de Olavide , Seville , Spain |
| AuthorAffiliation_xml | – name: 2 Instituto de la Grasa (CSIC), Campus Universitario Pablo de Olavide , Seville , Spain – name: 1 Department of Biochemistry and Molecular Biophysics, Kansas State University , Manhattan, KS , United States – name: 4 Departamento de Genética, Facultad de Biología, Universidad de Sevilla , Seville , Spain – name: 3 Department of Molecular and Cellular Biology, University of Guelph , Guelph, ON , Canada |
| Author_xml | – sequence: 1 givenname: Jose A. surname: Aznar-Moreno fullname: Aznar-Moreno, Jose A. – sequence: 2 givenname: Rosario surname: Sánchez fullname: Sánchez, Rosario – sequence: 3 givenname: Satinder K. surname: Gidda fullname: Gidda, Satinder K. – sequence: 4 givenname: Enrique surname: Martínez-Force fullname: Martínez-Force, Enrique – sequence: 5 givenname: Antonio J. surname: Moreno-Pérez fullname: Moreno-Pérez, Antonio J. – sequence: 6 givenname: Mónica surname: Venegas Calerón fullname: Venegas Calerón, Mónica – sequence: 7 givenname: Rafael surname: Garcés fullname: Garcés, Rafael – sequence: 8 givenname: Robert T. surname: Mullen fullname: Mullen, Robert T. – sequence: 9 givenname: Joaquín J. surname: Salas fullname: Salas, Joaquín J. |
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| Cites_doi | 10.1007/s00425-005-1502-z 10.1038/nprot.2007.360 10.1007/978-1-4899-1766-9-8 10.1111/ppl.12107 10.1038/nmeth.3213 10.1105/tpc.17.00397 10.1006/jmbi.2000.3903 10.1199/tab.0133 10.1093/emboj/21.11.2616 10.1371/journal.pone.0024699 10.1016/j.phytochem.2010.03.015 10.1146/annurev.arplant.48.1.109 10.1002/pmic.200700810 10.1074/jbc.M510945200 10.1007/s11103-008-9392-7 10.1016/0003-2697(76)90527-3 10.1007/BF00201039 10.1007/s00253-018-8770-6 10.1105/tpc.107.057679 10.3389/fpls.2012.00007 10.1105/tpc.008946 10.1002/jcc.21797 10.1038/76776 10.1006/jmbi.2000.4315 10.1111/j.1365-313X.2010.04396.x 10.1110/ps.8.5.978 10.1074/jbc.M311305200 10.1002/0471143030.cb0107s19 10.1007/BF00197585 10.1016/j.plaphy.2010.10.002 10.1093/nar/gkr366 10.1016/j.plaphy.2006.09.017 10.1104/pp.123.2.637 10.1007/s00425-013-2003-0 10.1074/jbc.M411351200 10.1074/jbc.271.7.3417 10.3389/fpls.2011.00118 10.1016/S0981-9428(00)00758-0 10.1111/j.1399-3054.1997.tb01066.x 10.1007/s00425-016-2521-7 10.1016/S0003-9861(02)00017-6 10.1093/bioinformatics/btn221 10.1021/bi00198a003 10.1016/S0981-9428(02)01386-4 10.1006/meth.2001.1262 10.1038/nprot.2007.132 10.1006/abbi.1995.1081 10.1105/tpc.7.3.359 10.1186/1471-2229-7-1 10.1002/jcc.20084 10.1016/S0981-9428(01)01337-7 10.1021/acschembio.7b00641 10.1002/elps.1150181505 10.1016/j.plaphy.2007.09.003 10.1105/tpc.107.057851 10.1016/j.phytochem.2014.08.014 10.1371/journal.pone.0010098 10.1016/S1570-0232(02)00767-5 10.1038/s41467-018-03310-z 10.1016/0003-2697(78)90046-5 10.1007/BF00196575 10.1385/1-59259-890-0:571 10.1007/s00425-014-2162-7 |
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| Copyright | Copyright © 2018 Aznar-Moreno, Sánchez, Gidda, Martínez-Force, Moreno-Pérez, Venegas Calerón, Garcés, Mullen and Salas. 2018 Aznar-Moreno, Sánchez, Gidda, Martínez-Force, Moreno-Pérez, Venegas Calerón, Garcés, Mullen and Salas |
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| Keywords | FatB FatA acyl-ACP thioesterase Helianthus annuus protein location sunflower |
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| References | Serrano-Vega (B56) 2003; 786 Feng (B18) 2017; 12 Jing (B32) 2018; 9 Heckman (B27) 2007; 4 Mayer (B46) 2007; 7 Moreno-Pérez (B49) 2014; 239 González-Thuillier (B22) 2015; 241 Hara (B26) 1978; 90 Dörmann (B12) 1995; 1 Brandizzi (B5) 2003; 19 Koo (B36) 2004; 279 Miao (B47) 2007; 2 Ghosh (B21) 2007; 45 Breuers (B6) 2012; 3 Cantisán (B8) 2000; 38 Kang (B34) 1996; 199 Krogh (B37) 2001; 305 Eccleston (B14) 1996; 198 Jain (B30) 2008; 8 Bonaventure (B3) 2003; 15 Guex (B25) 1997; 18 Heins (B28) 2002; 21 Jones (B33) 1995; 7 Ohlrogge (B50) 1997; 48 Li (B39) 2000; 7 Lawson (B38) 1994; 33 Mayer (B45) 2005; 280 Emanuelsson (B16) 1999; 8 Jha (B31) 2006; 44 Grosdidier (B23); 32 Salas (B53) 2002; 403 Yuan (B63) 1996; 271 Facciotti (B17) 1998; 100 Sánchez-García (B54) 2010; 71 Voelker (B59) 1996; 18 Machettira (B43) 2012; 2 Gasteiger (B20) 2005 Lingard (B41) 2008; 20 Rodríguez-Rodríguez (B52) 2014; 107 Schaffer (B55) 1997; 4 Xiao (B61) 2008; 68 Aznar-Moreno (B2) 2016; 244 Dhanoa (B11) 2010; 5 Zhao (B64) 2010; 64 Livak (B42) 2001; 25 Martínez-Force (B44) 2002; 40 Yang (B62) 2015; 12 Emanuelsson (B15) 2000; 300 Feng (B19) 2018; 102 Li-Beisson (B40) 2010 Viklund (B58) 2008; 24 Kato (B35) 1972 Grosdidier (B24); 39 Burrell (B7) 1994; 194 Moreno-Pérez (B48) 2011; 49 Dörmann (B13) 2000; 123 Wang (B60) 2017; 29 Chen (B9) 2008; 20 Pettersen (B51) 2004; 25 Chen (B10) 2006; 281 Aznar-Moreno (B1) 2014; 3 Serrano-Vega (B57) 2005; 221 Bradford (B4) 1976; 72 Huynh (B29) 2002; 40 |
| References_xml | – volume: 221 start-page: 868 year: 2005 ident: B57 article-title: Cloning, characterization and structural model of FatA-type thioesterase from sunflower seeds (Helianthus annuus L.). publication-title: Planta doi: 10.1007/s00425-005-1502-z – volume: 2 start-page: 2348 year: 2007 ident: B47 article-title: Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells. publication-title: Nat. Protoc. doi: 10.1038/nprot.2007.360 – volume: 18 start-page: 111 year: 1996 ident: B59 article-title: Plant acyl-ACP thioesterases: chain-length determining enzymes in plant fatty acid biosynthesis. publication-title: Genet. Eng. doi: 10.1007/978-1-4899-1766-9-8 – volume: 3 start-page: 363 year: 2014 ident: B1 article-title: Sunflower (Helianthus annuus) long-chain- acyl-coenzyme A synthetases expressed at high levels in developing seeds. publication-title: Physiol. Plant. doi: 10.1111/ppl.12107 – volume: 12 start-page: 7 year: 2015 ident: B62 article-title: The I-TASSER suite: protein structure and function prediction. publication-title: Nat. Methods doi: 10.1038/nmeth.3213 – volume: 29 start-page: 1678 year: 2017 ident: B60 article-title: A plastid phosphatidylglycerol lipase contributes to the export of acyl groups from plastids for seed oil biosynthesis. publication-title: Plant Cell doi: 10.1105/tpc.17.00397 – volume: 300 start-page: 1005 year: 2000 ident: B15 article-title: Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.3903 – year: 2010 ident: B40 article-title: “Acyl-lipid metabolism,” publication-title: The Arabidopsis Book doi: 10.1199/tab.0133 – volume: 21 start-page: 2616 year: 2002 ident: B28 article-title: The preprotein conducting channel at the inner envelope membrane of plastids. publication-title: EMBO J. doi: 10.1093/emboj/21.11.2616 – volume: 100 start-page: 167 year: 1998 ident: B17 article-title: Molecular dissection of the plant acyl-acyl carrier protein thioesterases. publication-title: Fett Lipid doi: 10.1371/journal.pone.0024699 – volume: 71 start-page: 860 year: 2010 ident: B54 article-title: Acyl-ACP thioesterase from castor (Ricinus communis L.): an enzymatic system appropriate for high rates of oil synthesis and accumulation. publication-title: Phytochemistry doi: 10.1016/j.phytochem.2010.03.015 – volume: 48 start-page: 109 year: 1997 ident: B50 article-title: Regulation of fatty acid synthesis. publication-title: Ann. Rev. Plant Physiol. Plant Mol. Biol. doi: 10.1146/annurev.arplant.48.1.109 – volume: 8 start-page: 3397 year: 2008 ident: B30 article-title: Purification and proteomic characterization of plastids from Brassica napus developing embryos. publication-title: Proteomics doi: 10.1002/pmic.200700810 – volume: 281 start-page: 5726 year: 2006 ident: B10 article-title: The PII signal transduction protein of Arabidopsis thaliana forms an arginine-regulated complex with plastid N-acetyl glutamate Kinase. publication-title: J. Biol. Chem. doi: 10.1074/jbc.M510945200 – volume: 68 start-page: 571 year: 2008 ident: B61 article-title: Arabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly localized to the cytosol and ACBP4 depletion affects membrane lipid composition. publication-title: Plant Mol. Biol. doi: 10.1007/s11103-008-9392-7 – volume: 72 start-page: 248 year: 1976 ident: B4 article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. publication-title: Anal. Biochem. doi: 10.1016/0003-2697(76)90527-3 – volume: 194 start-page: 95 year: 1994 ident: B7 article-title: Genetic manipulation of 6 phosphofructokinase in potato tubers. publication-title: Planta doi: 10.1007/BF00201039 – volume: 102 start-page: 3173 year: 2018 ident: B19 article-title: Tuning of acyl-ACP thioesterase activity directed for tailored fatty acid synthesis. publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-018-8770-6 – volume: 20 start-page: 1567 year: 2008 ident: B41 article-title: Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes. publication-title: Plant Cell doi: 10.1105/tpc.107.057679 – volume: 3 year: 2012 ident: B6 article-title: Dynamic remodeling of the plastid envelope membranes–a tool for chloroplast envelope in vivo localizations. publication-title: Front. Plant Sci. doi: 10.3389/fpls.2012.00007 – volume: 15 start-page: 1020 year: 2003 ident: B3 article-title: Disruption of the FATB gene in Arabidopsis demonstrates an essential role of saturated fatty acids in plant growth. publication-title: Plant Cell doi: 10.1105/tpc.008946 – volume: 32 start-page: 2149 ident: B23 article-title: Fast docking using the CHARMM force field with EADock DSS. publication-title: J. Comput. Chem. doi: 10.1002/jcc.21797 – volume: 7 start-page: 555 year: 2000 ident: B39 article-title: Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/76776 – volume: 305 start-page: 567 year: 2001 ident: B37 article-title: Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.4315 – volume: 64 start-page: 1048 year: 2010 ident: B64 article-title: Insertional mutant analysis reveals that long-chain acyl-CoA synthetase 1 (LACS1) but not LACS8, functionally overlaps with LACSp in Arabidopsis seed oil biosynthesis. publication-title: Plant J. doi: 10.1111/j.1365-313X.2010.04396.x – volume: 8 start-page: 978 year: 1999 ident: B16 article-title: ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. publication-title: Protein Sci. doi: 10.1110/ps.8.5.978 – volume: 279 start-page: 16101 year: 2004 ident: B36 article-title: On the export of fatty acids from the chloroplast. publication-title: J. Biol. Chem. doi: 10.1074/jbc.M311305200 – volume: 19 start-page: 1 year: 2003 ident: B5 article-title: BY-2 cells: culture and transformation for live cell imaging. publication-title: Curr. Prot. Cell Biol. doi: 10.1002/0471143030.cb0107s19 – volume: 198 start-page: 46 year: 1996 ident: B14 article-title: Medium-chain fatty acid biosynthesis and utilization in Brassica napus plants expressing lauroyl-acyl carrier protein thioesterase. publication-title: Planta doi: 10.1007/BF00197585 – volume: 49 start-page: 82 year: 2011 ident: B48 article-title: Acyl-ACP thioesterase from macadamia (Macadamia tetraphylla) nuts: cloning, characterization and their impact on oil composition. publication-title: Plant Physiol. Biochem. doi: 10.1016/j.plaphy.2010.10.002 – volume: 39 start-page: W270 ident: B24 article-title: SwissDock, a protein-small molecule docking web service based on EADock DSS. publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkr366 – volume: 44 start-page: 645 year: 2006 ident: B31 article-title: Cloning and functional expression of an acyl-ACP thioesterase FatB type from Diploknema butyracea (Madhuca) seeds in Escherichia coli. publication-title: Plant Physiol. Biochem. doi: 10.1016/j.plaphy.2006.09.017 – volume: 123 start-page: 637 year: 2000 ident: B13 article-title: Accumulation of palmitate in Arabidopsis mediated by the acyl-acyl carrier protein thioesterase FATB1. publication-title: Plant Physiol. doi: 10.1104/pp.123.2.637 – volume: 239 start-page: 667 year: 2014 ident: B49 article-title: Effect of a mutagenized acyl-ACP thioesterase FATA allele from sunflower with improved activity in tobacco leaves and Arabidopsis seeds. publication-title: Planta doi: 10.1007/s00425-013-2003-0 – volume: 280 start-page: 3621 year: 2005 ident: B45 article-title: A structure model of the plant acyl-acyl carrier protein thioesterase FatB comprises two helix/4-stranted sheet domains, the N-terminal domain containing residues that affect specificity and the C-terminal domain containing catalytic residues. publication-title: J. Biol. Chem. doi: 10.1074/jbc.M411351200 – volume: 271 start-page: 3417 year: 1996 ident: B63 article-title: The catalytic cysteine and histidine in the plant acyl-acyl carrier protein thioesterases. publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.7.3417 – volume: 2 year: 2012 ident: B43 article-title: Protein-induced modulation of chloroplast membrane morphology. publication-title: Front. Plant Sci. doi: 10.3389/fpls.2011.00118 – volume: 38 start-page: 377 year: 2000 ident: B8 article-title: Enzymatic studies of high stearic acid sunflower seed mutants. publication-title: Plant Physiol. Biochem. doi: 10.1016/S0981-9428(00)00758-0 – volume: 4 start-page: 800 year: 1997 ident: B55 article-title: Inhibition of fructokinase and sucrose synthase by cytosolic levels of fructose in young tomato fruit undergoing transient starch synthesis. publication-title: Physiol. Plant. doi: 10.1111/j.1399-3054.1997.tb01066.x – volume: 244 start-page: 479 year: 2016 ident: B2 article-title: Acyl carrier proteins from sunflower (Helianthus annuus L.) seeds and their influence on FatA and FatB acyl-ACP thioesterase activities. publication-title: Planta doi: 10.1007/s00425-016-2521-7 – volume: 403 start-page: 25 year: 2002 ident: B53 article-title: Characterization of substrate specificity of plant FatA and FatB acyl-ACP thioesterases. publication-title: Arch. Biochem. Biophys. doi: 10.1016/S0003-9861(02)00017-6 – volume: 24 start-page: 1662 year: 2008 ident: B58 article-title: Improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. publication-title: Bioinformatics doi: 10.1093/bioinformatics/btn221 – volume: 33 start-page: 9382 year: 1994 ident: B38 article-title: Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. publication-title: Biochemistry doi: 10.1021/bi00198a003 – volume: 40 start-page: 383 year: 2002 ident: B44 article-title: Dynamic channelling during de novo fatty acid biosynthesis in Helianthus annuus seeds. publication-title: Plant Physiol. Biochem. doi: 10.1016/S0981-9428(02)01386-4 – volume: 25 start-page: 402 year: 2001 ident: B42 article-title: Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method. publication-title: Methods doi: 10.1006/meth.2001.1262 – volume: 4 start-page: 924 year: 2007 ident: B27 article-title: Gene splicing and mutagenesis by PCR-driven overlap extension. publication-title: Nat. Prot. doi: 10.1038/nprot.2007.132 – volume: 1 start-page: 612 year: 1995 ident: B12 article-title: Cloning and expression in Escherichia coli of a novel thioesterase from Arabidopsis thaliana specific for long-chain acyl-acyl carrier proteins. publication-title: Biochem. Biophys. doi: 10.1006/abbi.1995.1081 – volume: 7 start-page: 359 year: 1995 ident: B33 article-title: Palmitoyl-acyl carrier protein (ACP) thioesterase and the evolutionary origin of plant acyl-ACP thioesterases. publication-title: Plant Cell doi: 10.1105/tpc.7.3.359 – volume: 7 year: 2007 ident: B46 article-title: Identification of amino acid residues involved in substrate specificity of plant acyl-ACP thioesterases using a bioinformatics-guided approach. publication-title: BMC Plant Biol. doi: 10.1186/1471-2229-7-1 – volume: 25 start-page: 1605 year: 2004 ident: B51 article-title: UCSF Chimera: a visualization system for exploratory research and analysis. publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 40 start-page: 1 year: 2002 ident: B29 article-title: Expression of a Gossypium hirsutum cDNA encoding a FatB palmitoyl-acyl carrier protein thioesterase in Escherichia coli. publication-title: Plant Physiol. Biochem. doi: 10.1016/S0981-9428(01)01337-7 – volume: 12 start-page: 2830 year: 2017 ident: B18 article-title: Structural insight into acyl-ACP thioesterase toward substrate specificity design. publication-title: ACS Chem. Biol. doi: 10.1021/acschembio.7b00641 – volume: 18 start-page: 2714 year: 1997 ident: B25 article-title: SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. publication-title: Electrophoresis doi: 10.1002/elps.1150181505 – volume: 45 start-page: 887 year: 2007 ident: B21 article-title: Characterization and cloning of a stearoyl/oleoyl specific fatty acyl-acyl carrier protein thioesterase from the seeds of Madhuca longifolia (latifolia). publication-title: Plant Physiol. Biochem. doi: 10.1016/j.plaphy.2007.09.003 – volume: 20 start-page: 1862 year: 2008 ident: B9 article-title: Sphingolipid long-chain base hydroxylation is important for growth and regulation of sphingolipid content and composition in Arabidopsis. publication-title: Plant Cell doi: 10.1105/tpc.107.057851 – volume: 107 start-page: 7 year: 2014 ident: B52 article-title: Acyl-ACP thioesterases from Camelina sativa: cloning, enzymatic characterization and implication in seed oil fatty acid composition. publication-title: Phytochemistry doi: 10.1016/j.phytochem.2014.08.014 – volume: 5 year: 2010 ident: B11 article-title: Distinct pathways mediate the sorting of tail-anchored proteins to the plastid outer envelope. publication-title: PLoS One doi: 10.1371/journal.pone.0010098 – volume: 786 start-page: 221 year: 2003 ident: B56 article-title: Cloning and expression of fatty acids biosynthesis key enzymes from sunflower (Helianthus annuus L.) in Escherichia coli. publication-title: J. Chromatogr. B doi: 10.1016/S1570-0232(02)00767-5 – volume: 9 year: 2018 ident: B32 article-title: Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase. publication-title: Nat. Commun. doi: 10.1038/s41467-018-03310-z – volume: 90 start-page: 420 year: 1978 ident: B26 article-title: Lipid extraction of tissues with a low-toxicity solvent. publication-title: Anal. Biochem. doi: 10.1016/0003-2697(78)90046-5 – volume: 199 start-page: 321 year: 1996 ident: B34 article-title: Metabolism of glucose-6-phosphate and utilization of multiple metabolites for fatty acid synthesis by plastids from developing oilseed rape embryos. publication-title: Planta doi: 10.1007/BF00196575 – start-page: 689 year: 1972 ident: B35 article-title: “Liquid suspension culture of tobacco cells,” publication-title: Ferment Technology Today – start-page: 571 year: 2005 ident: B20 article-title: “Protein identification and analysis tools on the ExPASy Server,” publication-title: The Proteomics Protocols Handbook doi: 10.1385/1-59259-890-0:571 – volume: 241 start-page: 43 year: 2015 ident: B22 article-title: Sunflower (Helianthus annuus) fatty acid synthase complex: enoyl-[acyl carrier protein]-reductase genes. publication-title: Planta doi: 10.1007/s00425-014-2162-7 |
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L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal... Sunflower seeds (Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period... Sunflower seeds ( Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period... |
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| Title | New Insights Into Sunflower (Helianthus annuus L.) FatA and FatB Thioesterases, Their Regulation, Structure and Distribution |
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