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  • 1
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Using two different experimental approaches—UV induced mitotic recombination and meiotic segregation—a fatty acid synthetase gene locus has been mapped on chromosome Fragment V of the Saccharomyces cerevisiae genetic map. This locus has been tentatively designated as fas1AB since it is a complex locus coding for at least two different fatty acid synthetase component enzymes, namely the β-hydroxyacid dehydratase and the enoyl reductase. According to the meiotic segregation patterns obtained, fas1AB is 41.6 centimorgans from ura1 and 35.7 centimorgans from trp3. Furthermore, the same criteria of mitotic sectoring and meiotic segregation indicate that the second known fatty acid synthetase gene cluster in yeast is genetically unlinked to fas1AB or to any other of the known genetic loci on Fragment V.
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  • 2
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Of 43 non-complementing alleles studied of the Saccharomyces cerevisiae fatty acid synthetase locus fas 1, 27 are reverted by external suppressors whereas 16 are susceptible only to intragenic suppression. Of the externally suppressible mutants 12 are reverted by both, amber and ochre suppressors, another 12 only by amber suppressors, and 3 are not suppressed by either of them. According to their response to the acridine mustard, ICR-191, one of the mutants not suppressible by external suppressors appears to be a frameshift mutation, whereas the others are suggested to be missense mutations. By X-ray induced mitotic recombination a genetic fine structure map of the complementing as well as of the noncomplementing fas 1-alleles was constructed. It was found that the alleles of the non-pleiotropic complementation groups II, Va, Vb and Vc map at distinct and characteristic regions within fas 1, each of them covering 9.8, 13.5, 5.3 and 1.6 X-ray map units, respectively. On the other hand, the non-complementing fas 1-alleles are distributed randomly over the entire locus, no matter whether they were nonsense or missense mutations. These non-complementing alleles are spread over a DNA region of 72 X-ray map units length and all the complementing alleles studied map within this region. These results suggest that fas 1 encodes only one, functionally complex, polypeptide chain.
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  • 3
    ISSN: 1617-4623
    Keywords: Multifunctional enzyme ; Cluster gene ; Nucleotide sequence ; Yeast transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary FAS1, the structural gene of the pentafunctional fatty acid synthetase subunit β in Saccharomyces cerevisiae has been sequenced. Its reading frame represents an intronfree nucleotide sequence of 5,535 base pairs, corresponding to a protein of 1,845 amino acids with a molecular weight of 205,130 daltons. In addition to the coding sequence, 1,468 base pairs of its 5′-flanking region were determined. S1 nuclease mapping revealed two transcriptional initiation sites, 5 and 36 base pairs upstream of the translational start codon. Within the flanking sequences two TATATAAA boxes, several A-rich and T-rich blocks and a TAG-...TATGTT...TATGTT...TTT sequence were found and are discussed as transcriptional initiation and termination signals, respectively. The order of catalytic domains in the cluster gene was established by complementation of defined fas1 mutants with overlapping FAS1 subclones. Acetyl transferase (amino acids 1–468) is located proximal to the N-terminus of subunit β, followed by the enoyl reductase (amino acids 480–858), the dehydratase (amino acids 1,134–1,615) and the malonyl/palmityl transferase (amino acids 1,616–1,845) domains. One major inter-domain region of about 276 amino acids with so far unknown function was found between the enoyl reductase and dehydratase domains. The substrate-binding serine residues of acetyl, malonyl and palmityl transferases were identified within the corresponding domains. Significant sequence homologies exist between the acyl transferase active sites of yeast and animal fatty acid synthetases. Similarly, a putative sequence of the enoyl reductase active site was identified.
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  • 4
    ISSN: 0570-0833
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
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  • 5
    ISSN: 0749-503X
    Keywords: Multifunctional FAS2 gene ; Chromosome hybridisation ; spo11 mapping ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The trifunctional FAS2 gene encoding subunits α of the Saccharomyces cerevisiae fatty acid synthetase complex was mapped on the left arm of chromosome XVI 24 centinorgans proximal to GAL4 and 39 centimorgans distal and PEP4 relative to the centromere. Mapping was achieved by three-independent methods: meiotic co-segragation of FAS2 and ARO7 in recombination-deficient spo11-mutants; tetrad analysis of crosses between FAS2, GAL4 and PEP4; and Southern hybridization of purified FAS2 DBA with individual yeast chromosomes separated by pulsed-field gel electrophoresis.
    Additional Material: 2 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
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  • 7
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
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  • 8
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary From a Saccharomyces cerevisiae gene bank contained in the novel yeast cosmid shuttle vector pMS201 the fatty acid synthetase (FAS) genes FAS1 and FAS2 were isolated. FAS clones were identified by in situ colony hybridization using two yeast DNA probes apparently capable of producing avian FAS cross-reacting material (J. Carbon, personal communication). Classification as FAS1 or FAS2 clones was achieved by their specific transformation of fas1 and fas2 yeast mutants. By transcription mapping FAS1 was assigned to about 5.3 kb within 14.8 kb of chromosomal DNA covered by two genomically adjacent BamHI fragments. The FAS2 gene was localized on a single BamHI fragment of 25 kb. One of the FAS clones (FAS2) produces immunologically cross-reacting material in Escherichia coli. High frequency transformation of fas1 mutants was only observed with one subclone, pMS3021, containing the intact FAS1 locus. Other DNA segments cloned in the same self-replicating vector but representing only part of FAS1 exhibited drastically lower transformation rates. As evident from this and from FAS1/TRP1-contransformation rates only the intact FAS1 gene in pMS3021 is capable of fas1-mutant complementation. With partial FAS1 genes, even when coding for an intact equivalent of the mutated domain, their chromosomal integration is necessary for the expression of FAS. In intergrative transformants the coexistence of integrated and autonomously replicating plasmid DNA was demonstrated. Both, the extrachromosomal and chromosomally integrated FAS DNA was mitotically unstable. Transformation studies using subcloned FAS1 DNA segments revealed the relative locations of the enoyl reductase and dehydratase domains within this pentafunctional cluster gene.
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  • 9
    ISSN: 1617-4623
    Keywords: Yeast fatty acid synthetases ; Yarrowia lipolytica/Saccharomyces cerevisiae FAS1 sequence comparison ; S. cerevisiae FAS1 sequence correction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The fatty acid synthetase (FAS) gene FAS1 of the alkane-utilizing yeast Yarrowia lipolytica was cloned and sequenced. The gene is represented by an intron-free reading frame of 6228 by encoding a protein of 2076 amino acids and 229980 Da molecular weight. This protein exhibits a 58% sequence similarity to the corresponding Saccharomyces cerevisiae FAS β-subunit. The sequential order of the five FAS1-encoded enzyme domains, acetyl transferase, enoyl reductase, dehydratase and malonyl/palmityl-transferase, is co-linear in both organisms. This finding agrees with available evidence that the functional organization of FAS genes is similar in related organisms but differs considerably between unrelated species. In addition, previously reported conflicting data concerning the 3′ end of S. cerevisiae FAS1 were re-examined by genomic and cDNA sequencing of the relevant portion of the gene. Thereby, the translational stop codon was shown to lie considerably downstream of both published termination sites. The S. cerevisiae FAS1 gene thus has a corrected length of 6153 by and encodes a protein of 2051 amino acids and 228667 Da molecular weight.
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  • 10
    ISSN: 1617-4623
    Keywords: Fatty acid synthetase ; Brevibacterium ammoniagenes/Saccaromyces cerevisiae ; Gene fusion ; Multifunctional proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Brevibacterium ammoniagenes fatty acid synthetase (FAS) gene was isolated from a series of overlapping clones by both immunological and plaque hybridization screening of two independent gene libraries. From the isolated DNA a contiguous segment of 10549 by was sequenced in both directions. The sequenced DNA contained a very long (9312 nucleotides) open reading frame coding for a protein of 3104 amino acids and with a molecular mass of 327466 daltons. Based on characteristic sequence motifs known from other FAS systems, seven different FAS active centres were identified at distinct locations within the polypeptide chain. Only one component enzyme, the 3-hydroxydecanoyl β,γ-dehydratase, has not yet been localized definitively within the gene. Translation is presumed to start from a GUG triplet located 25 nucleotides downstream of the transcriptional initiation site. There is a canonical Shine-Dalgarno sequence just before this start codon. Comparison of the B. ammoniagenes FAS sequence with those of other known fatty acid synthetases revealed a particularly high degree of similarity to the products of the two yeast genes, FAS1 and FAS2 (30% identical and 46% identical plus closely related amino acids). This similarity extends over the entire length of the genes and involves not only the primary sequences of individual component enzymes but also their sequential order within the multifunctional proteins. These data, together with those on the structure of other fatty acid synthetases are interpreted in terms of a contribution of both primary structure and subunit cooperation to a conserved topology of functional domains common to all type I FAS complexes.
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