Characterization of a genomic and cDNA clone coding for the thioesterase domain and 3' noncoding region of the chicken liver fatty acid synthase gene

Kasturi, R; Chirala, Subrahmanyam S.; Pazirandeh, Mehran; Wakil, Salih J.

doi:10.1021/bi00420a029

Cited by 15 publications

(8 citation statements)

References 37 publications

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“…Comparison of the amino acid sequence of rape thioesterase with long chain thioesterases from animal [2,11,17] or yeast [3] systems reveals no significant homologies, in agreement with observations made with the safflower thioesterase [ 12]. The GXSXG serine active site consensus sequence [ 1 ] present in animal thioesterases and in other acyl transferases and lipases is not present in the rape thioesterase sequence, again in agreement with findings with the safflower enzyme [12].…”

Section: H E L Q I T L D Y R R E C Q D D I V D S L T Se D I S K L G Tsupporting

confidence: 81%

Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones

et al. 1993

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Acyl-ACP thioesterases are involved in regulating chain termination of fatty acid biosynthesis in plant systems. Previously, acyl-ACP thioesterase purified from Brassica napus seed tissue has been shown to have a high preference for hydrolysing oleoyl-ACP. Here, oligonucleotides derived from B. napus oleoyl-ACP thioesterase protein sequence data have been used to isolate two acyl-ACP thioesterase clones from a B. napus embryo cDNA library. The two clones, pNL2 and pNL3, contain 1642 bp and 1523 bp respectively and differ in the length of their 3' non-coding regions. Both cDNAs contain open reading frames of 366 amino acids which encode for 42 kDa polypeptides. Mature rape thioesterase has an apparent molecular weight of 38 kDa on SDS-PAGE and these cDNAs therefore encode for precursor forms of the enzyme. This latter finding is consistent with the expected plastidial location of fatty acid synthase enzymes. Northern blot analysis shows thioesterase mRNA size to be ca. 1.6 kb and for the thioesterase genes to be highly expressed in seed tissue coincident with the most active phase of storage lipid synthesis. There is some sequence heterogeneity between the two cDNA clones, but overall they are highly homologous sharing 95.7% identity at the DNA level and 98.4% identity at the amino acid level. Some sequence heterogeneity was also observed between the deduced and directly determined thioesterase protein sequences. Consistent with the observed sequence heterogeneity was Southern blot data showing B. napus thioesterase to be encoded by a small multi-gene family.

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Section: H E L Q I T L D Y R R E C Q D D I V D S L T Se D I S K L G Tsupporting

confidence: 81%

Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones

et al. 1993

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“…Several reports indicated that the mutations in FASN gene were associated with (Bhuiyan et al, 2009;Lee et al, 2010;Zhang et al, 2008). Also, the polymorphisms in chicken FASN gene have been reported by Marrube et al (2004) and this gene is located on chromosome 18 and had three TE domains in exons 40, 41 and 42 (Kasturi et al, 1988).…”

Section: Introductionmentioning

confidence: 90%

“…In case of FASN gene in chicken liver, Kasturi et al (1988) observed that TE domain was located in exon 40-42 that might be also responsible for fatty acid analysis in chicken. In addition, the lack of association might also be highlighted by the sample size that has often failed to validate the analysis.…”

Section: Fasn and Scd Gene Effects To Fa Compositionmentioning

confidence: 99%

Association of FASN and SCD genes with fatty acid composition in broilers

Maharani¹,

Seo²,

Choi³

et al. 2013

Korean Journal of Agricultural Science

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: Fatty acids (FAs) were considered in activating nuclear hormone receptors that play significant roles in the cellular lipid metabolism by the regulation of several genes. Previously, fatty acid synthase (FASN) and stearoyl-CoA desaturase (SCD) genes have been known to regulating the FA metabolism. In this study, associations of FASN and SCD genes with fatty acid (FA) composition in broilers were investigated. Tissue samples from 95 Cobb 500 broilers were used for DNA extraction. The g.1222 A>G SNP located in intron 42 of FASN gene and 2 SNPs in SCD gene, one in exon 2 (g.3728A>G) and the other in exon 4 (g.12903G>A), were subjected for genotyping using PCR-RFLP method. One of the SNPs in SCD gene, SNP g.3728A>G had significant association with myristoleic acid (C14:1; P<0.05), palmitic acid (C16:0; P<0.05), palmitoleic acid (C16:1; P<0.05) and saturated FA (SFA; P<0.05). However, the SNP g.1222A>G in FASN gene had only suggestive association with arachidic acid (C20:0; P=0.08). The findings in this study suggest that the SNP in exon 2 of SCD gene can be used as a molecular marker for selecting birds having desirable FA composition in broilers.

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“…Isolation and Characterization of Genomic Clones-The human liver genomic library was screened at a density of 3,000 plaques/90-mm plate by using a [␣-32 P]dCTP-labeled 485-bp human FAS cDNA fragment, Try3-27 (25), as a probe as described previously (26). Approximately 2 ϫ 10 6 plaques were screened.…”

Section: Methodsmentioning

confidence: 99%

Human Fatty-acid Synthase Gene

Hsu

Chirala

Wakil

1996

Journal of Biological Chemistry

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We have isolated and sequenced a genomic clone coding for the first three exons and the 5'-flanking region of the human fatty-acid synthase gene. The translation initiation site, ATG, is located in exon II. Primer extension and S1 nuclease analyses showed the presence of three transcription initiation (Ti) sites: Ti I, Ti II, and Ti III. The Ti I site is mapped to the beginning of the untranslated exon I and preceded by a promoter with recognizable TATA and CAAT boxes. The Ti II and Ti III sites are located in intron I, at 60 and 49 nucleotides upstream of the translation initiation site ATG in exon II, respectively. These two Ti sites are preceded by four putative Sp1 boxes, but lack TATA and CAAT boxes. Analysis of luciferase reporter gene expression in transient transfection assays confirmed the existence of two promoters. A 200-base pair 5'-flanking region, which has strong promoter activity comparable with that of the CMV promoter, is considered human fatty-acid synthase promoter I. In a wild-type human fatty-acid synthase-luciferase construct, in which promoter I and intron I are present in their natural configuration, the reporter gene activity is only 1% of that of promoter I. Deletion analysis showed the existence of promoter II, which is located in intron I immediately upstream of the Ti II site. The strength of promoter II is approximately th of that of promoter I in transient transfection assays. Further analysis of reporter gene constructs showed that promoter II inhibited the reporter gene activity of the wild-type construct that contained promoter I and intron I and that the spatial separation of the two promoters is important for this inhibition. A model is proposed based on the possibility that the assembly of transcription complexes on promoter II creates a "roadblock" and reduces the overall expression of the fatty-acid synthase gene by interfering with the progression of transcription from promoter I.

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Characterization of a genomic and cDNA clone coding for the thioesterase domain and 3' noncoding region of the chicken liver fatty acid synthase gene

Cited by 15 publications

References 37 publications

Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones

Isolation and characterization of two Brassica napus embryo acyl-ACP thioesterase cDNA clones

Association of FASN and SCD genes with fatty acid composition in broilers

Human Fatty-acid Synthase Gene

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