Molecular cloning of gene sequences for avian fatty acid synthase and evidence for nutritional regulation of fatty acid synthase mRNA concentration.

Morris, Sidney M.; Nilson, John H.; Jenik, Robert A.; Winberry, L; McDevitt, Michael A.; Goodridge, Alan G.

doi:10.1016/s0021-9258(19)81099-2

Cited by 69 publications

(9 citation statements)

References 38 publications

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“…The native enzyme (Mx ~500 000) isolated from animal cells consists of two such multifunctional polypeptides (Arslanian et al, 1976; Buckner & Kolattukudy, 1976;Stoops et al, 1979;Smith et al, 1985). The mRNA coding for the avian (Zehner et al, 1980;Morris, 1982) and rat mammary gland (Mattick et al, 1981) synthases was shown to be a single contiguous mRNA which can be translated to a protein of Mt 260000 that specifically binds to the anti-synthase antibodies and can Functional map and organization of the subunit proteins of the chicken liver fatty acid synthase. The two subunits with their domains I, II, and III are drawn in an antiparallel arrangement (subunit division) so that two sites of palmitate synthesis are constructed (functional division).…”

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Fatty acid synthase, a proficient multifunctional enzyme

1989

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Fatty acid synthase, a proficient multifunctional enzyme

1989

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“…The activity and concentration of the animal fatty acid synthase vary depending upon the nutritional, hormonal, and developmental status (Wakil et al, 1983; Fischer & Goodridge, 1978; Joshi & Aranda, 1979; Kasturi & Joshi, 1982;Kasturi et al, 1984;Student et al, 1980;Weiss et al, 1980). The changes in the synthase activity and content under these various conditions are due in part to alterations in the rate of enzyme synthesis (Zehner et al, 1977; Fischer & Goodridge, 1978;Joshi & Aranda, 1979;Morris et al, 1982;Goodridge et al, 1984;Nepokroeff et al, 1984). Such changes are accompanied or preceded by corresponding changes in the levels of fatty acid synthase mRNA (Morris et al, 1982(Morris et al, , 1984Goodridge et al, 1984) suggesting that the regulation of synthase mRNA is predominantly at the level of gene transcription (Back et al, 1986).…”

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“…The changes in the synthase activity and content under these various conditions are due in part to alterations in the rate of enzyme synthesis (Zehner et al, 1977; Fischer & Goodridge, 1978;Joshi & Aranda, 1979;Morris et al, 1982;Goodridge et al, 1984;Nepokroeff et al, 1984). Such changes are accompanied or preceded by corresponding changes in the levels of fatty acid synthase mRNA (Morris et al, 1982(Morris et al, , 1984Goodridge et al, 1984) suggesting that the regulation of synthase mRNA is predominantly at the level of gene transcription (Back et al, 1986). However, the precise molecular mechanism by which the changes in synthase protein are regulated is not yet known.…”

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“…The 1 Abbreviations: FAS, fatty acid synthase; bp, base pair(s); kb, kilobase(s); kbp, kilobase pair(s); SDS, sodium dodecyl sulfate; TE1 and TE2, oligonucleotide probes; TE, thioesterase. 0006-2960/88/0427-7778S01.50/0 © 1988 American Chemical Society synthase mRNAs of goose uropygial gland and liver (Zehner et al, 1980;Morris et al, 1982;Back et al, 1986) and lactating rat mammary gland (Mattick et al, 1981) are estimated to be about 10-16 kb, which is about twice the number of nucleotides required for the 2300 amino acids needed for the subunit protein synthesis. The excess nucleotides present in the mRNA would have to be distributed between the 5' and 3' untranslated regions of the molecule.…”

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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

Kasturi¹,

Chirala²,

Pazirandeh³

et al. 1988

Biochemistry

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The fatty acid synthase (FAS) of animal tissue is a dimer of two identical subunits, each with a Mr of 260,000. The subunit is a single multifunctional protein having seven catalytic activities and a site for binding of the prosthetic group 4'-phosphopantetheine. The mRNA coding for the subunit has an estimated size of 10-16 kb, which is about twice the number of nucleotides needed to code for the estimated 2300 amino acids. We have isolated a positive clone, lambda CFAS, containing FAS gene sequences by screening a chicken genomic library with a segment of a 3' untranslated region of goose fatty acid synthase cDNA clone, pGFAS3, as a hybridization probe. The DNA insert in lambda CFAS hybridizes with synthetic oligonucleotide probes prepared according to the known amino acid sequence of the thioesterase component of the chicken liver fatty acid synthase [Yang, C.-Y., Huang, W.-Y., Chirala, S., & Wakil, S.J. (1988) Biochemistry (preceding paper in this issue)]. Further characterization of the DNA insert shows that the lambda CFAS clone contains about a 4.7-kbp segment from the 3' end of the chicken FAS gene that codes for a portion of the thioesterase domain. Complete sequence analyses of this segment including S1 nuclease mapping, showed that the lambda CFAS clone contains the entire 3' untranslated region of the chicken FAS gene and three exons that code for 162 amino acids of the thioesterase domain from the COOH-terminal end of the fatty acid synthase. Using the exon region of the genomic clone, we were able to isolate a cDNA clone that codes for the entire thioesterase domain of chicken liver fatty acid synthase.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…RNA was extracted from the livers of white Peking ducks by a modification of the guanidine thiocyanate procedure (Chirgwin et al, 1979;Mori et al, 1979). A cDNA library was prepared from duck poly(A+) RNA essentially as described previously (Morris et al, 1982). A random array of colonies was prepared on nitrocellulose filters, replicated (Hanahan & Meselson, 1980), and screened with a 32P-labeled, single-stranded DNA probe synthesized from a goose cDNA cloned into M13mp8 (Winberry et al, 1983).…”

Section: Purification Of Malicmentioning

confidence: 99%

A cloned cDNA for duck malic enzyme detects abnormally large malic enzyme mRNAs in a strain of mice (Mod-1n) that does not express malic enzyme protein

Glynias¹,

Morris²,

Fantozzi³

et al. 1984

Biochemistry

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Sensitive immunochemical assays were used to measure the mass and rate of synthesis of malic enzyme protein in wild-type and Mod-1n mutant mice fed a high carbohydrate/low fat diet supplemented with thyroid hormone. Malic enzyme activity in the fed, wild-type mice was 100-fold higher than in starved, wild-type mice. Neither activity, mass, nor synthesis of malic enzyme could be detected in fed, mutant mice. However, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase responded to these dietary manipulations with normal or supranormal increases in activities, respectively, in mutant mice. A cDNA clone containing an almost complete copy of the mRNA for malic enzyme from duck liver was used to analyze poly(A+) RNA from C57BL/6J-DBA/2J hybrid mice that had been fasted and refed a high carbohydrate/low fat diet supplemented with thyroid hormone. The 32P-cDNA probe hybridized to two RNAs of 2250 and 2950 nucleotides. The same two RNAs were detected in RNA from starved mice except at much lower concentrations. A similar analysis of RNA from Mod-1n mice fed the high carbohydrate-thyroid diet also revealed two hybridizing RNAs but each was 700-800 nucleotides longer than its counterpart in wild-type mice. The abundance of malic enzyme mRNA in the fed, mutant mice was about the same as that in fed, wild-type mice. The mutant malic enzyme mRNAs also were present in RNA from starved mice but at much lower concentrations. These results suggest that the mutation responsible for the Mod-1n phenotype is in the structural gene for malic enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)

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Molecular cloning of gene sequences for avian fatty acid synthase and evidence for nutritional regulation of fatty acid synthase mRNA concentration.

Cited by 69 publications

References 38 publications

Fatty acid synthase, a proficient multifunctional enzyme

Fatty acid synthase, a proficient multifunctional enzyme

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

A cloned cDNA for duck malic enzyme detects abnormally large malic enzyme mRNAs in a strain of mice (Mod-1n) that does not express malic enzyme protein

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