Domestication of dairy yeast Kluyveromyces lactis: Transfer of the β-galactosidase (LAC4) and lactose permease (LAC12) gene cluster?

2005 ◽  
Vol 401 (1-6) ◽  
pp. 120-122 ◽  
Author(s):  
G. I. Naumov
2019 ◽  
Vol 29 (24) ◽  
pp. 4284-4290.e2 ◽  
Author(s):  
Javier A. Varela ◽  
Martina Puricelli ◽  
Raúl A. Ortiz-Merino ◽  
Romina Giacomobono ◽  
Stephanie Braun-Galleani ◽  
...  

2019 ◽  
Author(s):  
Javier A. Varela ◽  
Martina Puricelli ◽  
Raúl A. Ortiz-Merino ◽  
Romina Giacomobono ◽  
Stephanie Braun-Galleani ◽  
...  

2021 ◽  
Vol 37 (4) ◽  
pp. 43-50
Author(s):  
E.S. Naumova

A molecular genetic study of Kluyveromyces lactis yeasts isolated from various dairy products in the countries of the former Soviet Union and other regions of the world has been carried out. Based on physiological tests, four strains were selected that carry different LAC loci and are characterized by good fermentation intensity: VKM Y-1339 (LAC3), VKM Y-1333 (LAC3), NRRL Y-1118 (LAC1), and NRRL Y-1140 (LAC2). Eleven hybrids of the selected strains with different rates of lactose fermentation were obtained. No correlation was found between the intensity of lactose fermentation and the amino acid sequences of the LAC12 lactose permease gene of the LAC1, LAC2, and LAC3 loci. Apparently, a specific combination of genotypes of crossed strains has a more significant effect on the fermentation activity. The results obtained showed that inter-strain hybridization of K. lactis dairy yeast is an effective method for creating new strains with high fermentation capacity. Hybrids H2-3 (NRRL Y-1118 × VKM Y-1333) and H3-3 (NRRL Y-1140 × VKM Y-1333) with the highest ability to ferment lactose are of interest for further molecular genetic research and breeding programs. Key words: Kluyveromyces lactis, β-galactosidase, lactose permease, LAC4, LAC12, LAC1 locus, LAC2 locus, LAC3 locus, inter-strain hybridization, lactose fermentation, heterosis Acknowledgment - The authors are grateful to the Genomic Center of the Kurchatov Institute SRC---GosNIIgentika for sequencing the nucleotide sequences of the LAC12 genes for lactose permease on the Applied Biosystems 3730 automated analyzer. Funding - This work was supported by an internal grant from the National Research Center Kurchatov Institute (order of the National Research Center Kurchatov Institute No. 1779).


Genetics ◽  
1989 ◽  
Vol 123 (3) ◽  
pp. 477-484 ◽  
Author(s):  
Q Cheng ◽  
C A Michels

Abstract The MAL61 gene of Saccharomyces cerevisiae encodes maltose permease, a protein required for the transport of maltose across the plasma membrane. Here we report the nucleotide sequence of the cloned MAL61 gene. A single 1842 bp open reading frame is present within this region encoding the 614 residue putative MAL61 protein. Hydropathy analysis suggests that the secondary structure consists of two blocks of six transmembrane domains separated by an approximately 71 residue intracellular region. The N-terminal and C-terminal domains of 100 and 67 residues in length, respectively, also appear to be intracellular. Significant sequence and structural homology is seen between the MAL61 protein and the Saccharomyces high-affinity glucose transporter encoded by the SNF3 gene, the Kluyveromyces lactis lactose permease encoded by the LAC12 gene, the human HepG2 glucose transporter and the Escherichia coli xylose and arabinose transporters encoded by the xylE and araE genes, indicating that all are members of a family of sugar transporters and are related either functionally or evolutionarily. A mechanism for glucose-induced inactivation of maltose transport activity is discussed.


2018 ◽  
Vol 115 (43) ◽  
pp. 11030-11035 ◽  
Author(s):  
David J. Krause ◽  
Jacek Kominek ◽  
Dana A. Opulente ◽  
Xing-Xing Shen ◽  
Xiaofan Zhou ◽  
...  

Secondary metabolites are key in how organisms from all domains of life interact with their environment and each other. The iron-binding molecule pulcherrimin was described a century ago, but the genes responsible for its production in budding yeasts have remained uncharacterized. Here, we used phylogenomic footprinting on 90 genomes across the budding yeast subphylum Saccharomycotina to identify the gene cluster associated with pulcherrimin production. Using targeted gene replacements in Kluyveromyces lactis, we characterized the four genes that make up the cluster, which likely encode two pulcherriminic acid biosynthesis enzymes, a pulcherrimin transporter, and a transcription factor involved in both biosynthesis and transport. The requirement of a functional putative transporter to utilize extracellular pulcherrimin-complexed iron demonstrates that pulcherriminic acid is a siderophore, a chelator that binds iron outside the cell for subsequent uptake. Surprisingly, we identified homologs of the putative transporter and transcription factor genes in multiple yeast genera that lacked the biosynthesis genes and could not make pulcherrimin, including the model yeast Saccharomyces cerevisiae. We deleted these previously uncharacterized genes and showed they are also required for pulcherrimin utilization in S. cerevisiae, raising the possibility that other genes of unknown function are linked to secondary metabolism. Phylogenetic analyses of this gene cluster suggest that pulcherrimin biosynthesis and utilization were ancestral to budding yeasts, but the biosynthesis genes and, subsequently, the utilization genes, were lost in many lineages, mirroring other microbial public goods systems that lead to the rise of cheater organisms.


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