Functional Characterization of Two Structurally Novel Diacylglycerol Acyltransferase2 Isozymes Responsible for the Enhanced Production of Stearate-Rich Storage Lipid in Candida tropicalis SY005
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{"title"=>"Functional characterization of two structurally novel diacylglycerol acyltransferase2 isozymes responsible for the enhanced production of stearate-rich storage lipid in Candida tropicalis SY005", "authors"=>[{"first_name"=>"Prabuddha", "last_name"=>"Dey", "scopus_author_id"=>"36701035300"}, {"first_name"=>"Monami", "last_name"=>"Chakraborty", "scopus_author_id"=>"56140617000"}, {"first_name"=>"Maulik R.", "last_name"=>"Kamdar", "scopus_author_id"=>"55735120100"}, {"first_name"=>"Mrinal K.", "last_name"=>"Maiti", "scopus_author_id"=>"7005401626"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"372981637", "sgr"=>"84899622968", "issn"=>"19326203", "pmid"=>"24732323", "scopus"=>"2-s2.0-84899622968", "doi"=>"10.1371/journal.pone.0094472", "isbn"=>"1932-6203"}, "id"=>"30fb2f11-f8e0-3ef1-9105-871781f637d3", "abstract"=>"Diacylglycerol acyltransferase (DGAT) activity is an essential enzymatic step in the formation of neutral lipid i.e., triacylglycerol in all living cells capable of accumulating storage lipid. Previously, we characterized an oleaginous yeast Candida tropicalis SY005 that yields storage lipid up to 58% under a specific nitrogen-stress condition, when the DGAT-specific transcript is drastically up-regulated. Here we report the identification, differential expression and function of two DGAT2 gene homologues--CtDGAT2a and CtDGAT2b of this C. tropicalis. Two protein isoforms are unique with respect to the presence of five additional stretches of amino acids, besides possessing three highly conserved motifs known in other reported DGAT2 enzymes. Moreover, the CtDGAT2a and CtDGAT2b are characteristically different in amino acid sequences and predicted protein structures. The CtDGAT2b isozyme was found to be catalytically 12.5% more efficient than CtDGAT2a for triacylglycerol production in a heterologous yeast system i.e., Saccharomyces cerevisiae quadruple mutant strain H1246 that is inherently defective in neutral lipid biosynthesis. The CtDGAT2b activity rescued the growth of transformed S. cerevisiae mutant cells, which are usually non-viable in the medium containing free fatty acids by incorporating them into triacylglycerol, and displayed preferential specificity towards saturated acyl species as substrate. Furthermore, we document that the efficiency of triacylglycerol production by CtDGAT2b is differentially affected by deletion, insertion or replacement of amino acids in five regions exclusively present in two CtDGAT2 isozymes. Taken together, our study characterizes two structurally novel DGAT2 isozymes, which are accountable for the enhanced production of storage lipid enriched with saturated fatty acids inherently in C. tropicalis SY005 strain as well as in transformed S. cerevisiae neutral lipid-deficient mutant cells. These two genes certainly will be useful for further investigation on the novel structure-function relationship of DGAT repertoire, and also in metabolic engineering for the enhanced production of lipid feedstock in other organisms.", "link"=>"http://www.mendeley.com/research/functional-characterization-two-structurally-novel-diacylglycerol-acyltransferase2-isozymes-responsi", "reader_count"=>19, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>4, "Student > Postgraduate"=>1, "Other"=>1, "Student > Master"=>1, "Professor"=>1, "Unspecified"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>4, "Student > Postgraduate"=>1, "Other"=>1, "Student > Master"=>1, "Professor"=>1, "Unspecified"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Engineering"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>12, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>12}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>2}}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1463436"], "description"=>"<p>(A) Ethidium bromide-stained 12% polyacrylamide gel of RT-PCR products (80 bp and 86 bp) showing differential expression of two homologous genes, <i>CtDGAT2a</i> and <i>CtDGAT2b</i> at four different nitrogen-stress conditions i.e., carbon (C):nitrogen (N) 50∶1, 100∶1, 150∶1 and 200∶1. In first two conditions (50∶1 and 100∶1), only the <i>CtDGAt2a</i> was found to be expressed, whereas both genes expressed in 150∶1 and 200∶1. Bar diagram represents relative expression of the two CtDGAT2 transcripts, calculated after densitometric scanning of the gel picture. The star indicates undetectable expression of the CtDGAT2b transcript in first two conditions (C:N 50∶1 and 100∶1). (B) Multiple amino acid sequence allignment of both CtDGAT2a and CtDGAT2b isoforms along with other five representatives of DGAT2 reported. Three motifs with remarkable sequence conservation required for DGAT activity found in all DGAT2s are indicated by rectangular box. Two brown colored boxes represent the absence of the critical Cys residue involved in N-ethylmaleimide-mediated enzyme inhibition and the neutral lipid-binding domain FVLF in two CtDGAT2 isoforms with respect to the ScDGAT2. Other colored boxes indicate the presence of five (D1 to D5) unique stretches of amino acids found specifically in two CtDGAT2 isoforms. Five representatives of DGAT2 reported from other organisms are: AtDGAT2, <i>Arabidopsis thaliana</i> NP_566952; CeDGAT2, <i>Caenorhabditis elegans NP_507469.1</i>; MrDGAT2a, <i>Mortierella ramanniana AAK84179</i>; ScDGAT2, <i>Saccharomyces cerevisiae NP_014888</i>; VfDGAT2, <i>Vernonia fordi ABC94474</i>.</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "structurally", "ctdgat2", "isozymes", "sy005", "lipid"], "article_id"=>998432, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g001", "stats"=>{"downloads"=>0, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Identification_of_two_structurally_novel_CtDGAT2_isozymes_in_C_tropicalis_SY005_yeast_during_storage_lipid_production_/998432", "title"=>"Identification of two structurally novel CtDGAT2 isozymes in <i>C. tropicalis</i> SY005 yeast during storage lipid production.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463443", "https://ndownloader.figshare.com/files/1463444", "https://ndownloader.figshare.com/files/1463445", "https://ndownloader.figshare.com/files/1463446", "https://ndownloader.figshare.com/files/1463447", "https://ndownloader.figshare.com/files/1463448", "https://ndownloader.figshare.com/files/1463449"], "description"=>"<div><p>Diacylglycerol acyltransferase (DGAT) activity is an essential enzymatic step in the formation of neutral lipid i.e., triacylglycerol in all living cells capable of accumulating storage lipid. Previously, we characterized an oleaginous yeast <i>Candida tropicalis</i> SY005 that yields storage lipid up to 58% under a specific nitrogen-stress condition, when the DGAT-specific transcript is drastically up-regulated. Here we report the identification, differential expression and function of two <i>DGAT2</i> gene homologues- <i>CtDGAT2a</i> and <i>CtDGAT2b</i> of this <i>C. tropicalis</i>. Two protein isoforms are unique with respect to the presence of five additional stretches of amino acids, besides possessing three highly conserved motifs known in other reported DGAT2 enzymes. Moreover, the CtDGAT2a and CtDGAT2b are characteristically different in amino acid sequences and predicted protein structures. The CtDGAT2b isozyme was found to be catalytically 12.5% more efficient than CtDGAT2a for triacylglycerol production in a heterologous yeast system i.e., <i>Saccharomyces cerevisiae</i> quadruple mutant strain H1246 that is inherently defective in neutral lipid biosynthesis. The CtDGAT2b activity rescued the growth of transformed <i>S. cerevisiae</i> mutant cells, which are usually non-viable in the medium containing free fatty acids by incorporating them into triacylglycerol, and displayed preferential specificity towards saturated acyl species as substrate. Furthermore, we document that the efficiency of triacylglycerol production by CtDGAT2b is differentially affected by deletion, insertion or replacement of amino acids in five regions exclusively present in two CtDGAT2 isozymes. Taken together, our study characterizes two structurally novel DGAT2 isozymes, which are accountable for the enhanced production of storage lipid enriched with saturated fatty acids inherently in <i>C. tropicalis</i> SY005 strain as well as in transformed <i>S. cerevisiae</i> neutral lipid-deficient mutant cells. These two genes certainly will be useful for further investigation on the novel structure-function relationship of DGAT repertoire, and also in metabolic engineering for the enhanced production of lipid feedstock in other organisms.</p></div>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "characterization", "structurally", "diacylglycerol", "acyltransferase2", "isozymes", "enhanced", "stearate-rich", "lipid", "sy005"], "article_id"=>998439, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0094472.s001", "https://dx.doi.org/10.1371/journal.pone.0094472.s002", "https://dx.doi.org/10.1371/journal.pone.0094472.s003", "https://dx.doi.org/10.1371/journal.pone.0094472.s004", "https://dx.doi.org/10.1371/journal.pone.0094472.s005", "https://dx.doi.org/10.1371/journal.pone.0094472.s006", "https://dx.doi.org/10.1371/journal.pone.0094472.s007"], "stats"=>{"downloads"=>2, "page_views"=>26, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Functional_Characterization_of_Two_Structurally_Novel_Diacylglycerol_Acyltransferase2_Isozymes_Responsible_for_the_Enhanced_Production_of_Stearate_Rich_Storage_Lipid_in_Candida_tropicalis_SY005/998439", "title"=>"Functional Characterization of Two Structurally Novel Diacylglycerol Acyltransferase2 Isozymes Responsible for the Enhanced Production of Stearate-Rich Storage Lipid in <i>Candida tropicalis</i> SY005", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463442"], "description"=>"<p>(A) Nile red fluorescence confocal microscopy showing lipid body formation is restored in yeast QM cells albeit at different extent, upon expression of five deletion mutants of CtDGAT2b. (B) Differential complementation of the TAG-deficient phenotype of the yeast QM strain by enzymatic activities of five deleted constructs ΔD1(1–21), ΔD2(170–187), ΔD3(252–271), ΔD4(341–384) and ΔD5(481–571). Neutral lipid fractions were separated by TLC, and lipid spots were visualized as described in experimental methods. (C) Western blot showing the recombinant proteins of 60–63 kDa produced upon galactose induction of yeast QM cells transformed with the recombinant pYES2/CT plasmid carrying either the full length <i>CtDGAT2b</i> gene or the mutant ΔD4(341–384) or ΔD6(365–374) version. Immunodetection was carried out with mouse anti-His monoclonal antibody. (D) Schematic diagram showing the insertion and replacement of amino acids at a unique polyglutamic acid stretch of ten residues in the segment ΔD4(341–384) created mutants D7(364::365–376), D8(364::KKKKKKKKKK) and D9(364::AAAAAAAAAA). (E) Bar and line diagrams representing gravimetric measurement and Nile red fluorescence assay of lipid content in QM cells after expression of the full length CtDGAT2b and all the five deletion, one insertional and two replacement mutants; along with the WT and QM cells transformed with the non-recombinant plasmid as positive and negative controls, respectively. Fluorescence was measured at the stationary phase using 485nm (excitation) and 540 nm (emission) before and after the addition of Nile red dye, and expressed in arbitrary unit.</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "enzymatic", "mutated", "versions", "ctdgat2b", "qm"], "article_id"=>998438, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g007", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Differential_enzymatic_activity_of_various_mutated_versions_of_the_CtDGAT2b_towards_TAG_formation_in_S_cerevisiae_QM_strain_/998438", "title"=>"Differential enzymatic activity of various mutated versions of the CtDGAT2b towards TAG formation in <i>S. cerevisiae</i> QM strain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463439"], "description"=>"<p>(A) Western blot showing the recombinant protein of ∼ 63 kDa produced upon galactose induction of yeast QM cells transformed with the full length <i>CtDGAT2a</i> or <i>CtDGAT2b</i> gene expression cassette prepared in pYES2/CT plasmid. Immunodetection was carried out with mouse anti-His monoclonal antibody. (B) Nile red fluorescence confocal microscopy showing lipid body formation is restored in yeast QM cells upon expression of either CtDGAT2a (QM-CtDGAT2a) or CtDGAT2b (QM-CtDGAT2b). The yeast wild-type BY742 cells were used as positive control (WT), and the QM cells harboring the non-recombinant plasmid was used as negative control (QM-pYES2). (C) Complementation of the TAG-deficient phenotype of the yeast QM strain by expression of either CtDGAT2a or CtDGAT2b. Neutral lipid fractions were separated by TLC, and lipid spots were visualized as described in experimental methods. (D) Bar and line diagrams representing gravimetric measurement and Nile red fluorescence assay of lipid content in QM cells after expression of the full length CtDGAT2a and CtDGAT2b, along with the WT and QM cells transformed with the non-recombinant plasmid as positive and negative controls, respectively. Fluorescence was measured at the stationary phase using 485nm (excitation) and 540nm (emission) before and after the addition of Nile red dye, and expressed in arbitrary unit.</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "ctdgat2a", "ctdgat2b", "functionally", "qm", "catalytically"], "article_id"=>998435, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g004", "stats"=>{"downloads"=>4, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Both_CtDGAT2a_and_CtDGAT2b_are_functionally_active_to_produce_TAG_in_S_cerevisiae_QM_strain_and_the_CtDGAT2b_is_catalytically_more_active_/998435", "title"=>"Both CtDGAT2a and CtDGAT2b are functionally active to produce TAG in <i>S. cerevisiae</i> QM strain, and the CtDGAT2b is catalytically more active.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463438"], "description"=>"<p>(A) Predicted two-dimensional structure of CtDGAT2a and CtDGAT2b isoforms. Black circles indicate the differences between the two. (B) Three-dimensional structure of two molecular models prepared using MODELLER and validated using PROCHECK. The green model represents the CtDGAT2a, whereas the red model represents the CtDGAT2b. Structural overlapping of the two models created regions A, B, C and D of extra side chain loops, formed by amino acid residues approximately 425–435, 385–430, 450–500 and 365–375, respectively.</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "ctdgat2", "isoforms", "tertiary"], "article_id"=>998434, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g003", "stats"=>{"downloads"=>0, "page_views"=>19, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Two_CtDGAT2_isoforms_are_different_from_each_other_at_the_level_of_secondary_and_tertiary_structures_/998434", "title"=>"Two CtDGAT2 isoforms are different from each other at the level of secondary and tertiary structures.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463441"], "description"=>"<p>(A) Schematic diagram of the five deletion mutants- ΔD1 to ΔD5 of the full length <i>CtDGAT2b</i> gene corresponding to the five unique stretches of amino acids represented as D1 to D5 in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0094472#pone-0094472-g001\" target=\"_blank\">Figure 1B</a>. (B) Ethidium bromide-stained 1.2% agarose gel showing restriction enzymes (<i>Bam</i>HI+<i>Eco</i>RI) digestion profile of the recombinant pYES2 plasmid carrying either the full length <i>CtDGAT2b</i> gene or each of the five deleted versions of <i>CtDGAT2b</i> gene. (C) Growth pattern of QM yeast cells transformed with the individual gene construct carrying either the full length <i>CtDGAT2b</i> or each of the five deletion mutants, after 4 days of plating of yeast cells (O.D. 1) in different dilutions (10<sup>−2</sup> to 10<sup>−5</sup>).</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "mutagenesis", "followed", "mutated", "qm"], "article_id"=>998437, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g006", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Deletion_mutagenesis_of_the_CtDGAT2b_gene_followed_by_the_expression_of_each_mutated_version_in_S_cerevisiae_QM_strain_/998437", "title"=>"Deletion mutagenesis of the <i>CtDGAT2b</i> gene followed by the expression of each mutated version in <i>S. cerevisiae</i> QM strain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463440"], "description"=>"<p>(A) Growth rescue of transformed QM cells in oleic acid containing media. Yeast nitrogen base media was used for the growth of wild-type (WT) and non-transformed QM cells with dextrose and uracil, whereas raffinose and galactose with no uracil was used for the QM transformant (QM-pYES2 or QM-CtDGAT2b) to induce the expression of transgene. Two microliters of yeast cells (O.D. 1), after serial dilutions (10<sup>−1</sup>, 10<sup>−2</sup>, 10<sup>−3</sup>, 10<sup>−4</sup> and 10<sup>−5</sup>) were spotted on solid media without or with 0.025 mM and 0.5 M oleic acid. (B) Growth phenotype of QM cells harboring non-recombinant plasmid pYES2 (QM-pYES2) and recombinant plasmid with the <i>CtDGAT2b</i> gene (QM-CtDGAT2b) on solid media supplemented with three different fatty acids- α-linoleic acid (C18:3), arachidonic acid (C20:4), erucic acid (C22:1) after 4 days at 30°C. (C) Fatty acid composition of TAGs isolated from the wild-type yeast (WT) and transformed QM cells (QM-CtDGAT2b) grown in liquid media (i) without any free fatty acid, and supplemented with (ii) α-linolenic acid (ALA), (iii) arachidonic acid (ARA) and (iv) erucic acid (EA).</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "ctdgat2b", "qm", "rescues", "cells", "cytotoxic", "fatty"], "article_id"=>998436, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g005", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Enzymatic_activity_of_CtDGAT2b_in_S_cerevisiae_QM_strain_rescues_the_yeast_cells_from_the_cytotoxic_effect_due_to_free_fatty_acid_in_growth_medium_/998436", "title"=>"Enzymatic activity of CtDGAT2b in <i>S. cerevisiae</i> QM strain rescues the yeast cells from the cytotoxic effect due to free fatty acid in growth medium.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/1463437"], "description"=>"<p>Hydropathy plots were generated by Kyte & Dollite method (28). X-axis and Y-axis indicate number of amino acid residues and hydrophobicity, respectively. Two green outlined boxes (D3 and D4) in CtDGAT2 isoforms indicate the presence of unique hydrophilic stretch of amino acids exclusively present in CtDGAT2.</p>", "links"=>[], "tags"=>["Biochemistry", "biotechnology", "Applied microbiology", "Industrial microbiology", "genetics", "genomics", "microbiology", "Microbial physiology", "Microbial metabolism", "Microbial mutation", "Mycology", "Fungal biochemistry", "organisms", "fungi", "yeast", "hydropathy", "profiles", "ctdgat2a", "ctdgat2b", "dgat2s", "revealed", "uniqueness", "ctdgat2"], "article_id"=>998433, "categories"=>["Biological Sciences"], "users"=>["Prabuddha Dey", "Monami Chakraborty", "Maulik R. Kamdar", "Mrinal K. Maiti"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0094472.g002", "stats"=>{"downloads"=>2, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparison_of_hydropathy_profiles_of_CtDGAT2a_and_CtDGAT2b_with_DGAT2s_from_S_cerevisiae_and_V_fordii_revealed_uniqueness_of_two_CtDGAT2_isozymes_/998433", "title"=>"Comparison of hydropathy profiles of CtDGAT2a and CtDGAT2b with DGAT2s from <i>S. cerevisiae</i> and <i>V. fordii</i> revealed uniqueness of two CtDGAT2 isozymes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-14 03:28:16"}

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Relative Metric

{"start_date"=>"2014-01-01T00:00:00Z", "end_date"=>"2014-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences/Organisms", "average_usage"=>[310]}]}
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