Structural and functional analysis of the MAL1 locus of Saccharomyces cerevisiae.

We describe the isolation of a 22.6-kilobase fragment of DNA containing the MAL1 locus of Saccharomyces cerevisiae. Our results demonstrate that the MAL1 locus, like the MAL6 locus, is a complex locus containing three genes. These genes were organized similarly to their MAL6 counterparts. We refer to them as MAL11, MAL12, and MAL13 and show that they are functionally homologous to the MAL61 (encoding maltose permease), MAL62 (encoding maltase), and MAL63 (encoding the positive regulator) genes of the MAL6 locus. Transcription from each of the three genes was analyzed in a strain carrying the undisrupted MAL1 locus and in strains carrying single disruptions in each of the MAL1 genes. The MAL1 and MAL1 loci were found to be highly sequence homologous and conserved throughout the region containing these three genes. The strain used to isolate the MAL1 locus also carried the tightly linked SUC1 gene. The SUC1 gene was found to be located on the same 22.6-kilobase fragment containing the MAL1 locus and 5 kilobases from the 3' end of the MAL12 gene. The meaning of these results with regard to the mechanism of regulation of maltose fermentation is discussed.

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Repeated Family of Genes Controlling Maltose Fermentation in Saccharomyces carlsbergensis

Molecular and Cellular Biology ◽

10.1128/mcb.3.5.796-802.1983 ◽

1983 ◽

Vol 3 (5) ◽

pp. 796-802

Author(s):

Richard B. Needleman ◽

Corinne Michels

Keyword(s):

Genetic Analysis ◽

Structural Gene ◽

Regulatory Gene ◽

Regulatory Protein ◽

Physical Analysis ◽

Saccharomyces Carlsbergensis ◽

Maltose Permease ◽

Maltose Fermentation ◽

Complex Locus ◽

Dna Fragment

Maltose fermentation in Saccharomyces spp. requires the presence of any one of five unlinked genes: MAL1, MAL2, MAL3, MAL4 , or MAL6. Although the genes are functionally equivalent, their natures and relationships to each other are not known. At least three proteins are necessary for maltose fermentation: maltase, maltose permease, and a regulatory protein. The MAL genes may code for one or more of these proteins. Recently a DNA fragment containing a maltase structural gene has been cloned from a MAL6 strain, CB11, to produce plasmid pMAL9-26. We have conducted genetic and physical analyses of strain CB11. The genetic analysis has demonstrated the presence of two cryptic MAL genes in CB11, MAL1g and MAL3g (linked to MAL1 and to MAL3 , respectively), in addition to the MAL6 locus. The physical analysis, which used a subclone of plasmid pMAL9-26 as a probe, detected three Hin dIII genomic fragments with homology to the probe. Each fragment was shown to be linked to one of the MAL loci genetically demonstrated to be present in CB11. Our results indicate that the cloned maltase structural gene in plasmid pMAL9-26 is linked to MAL6. Since the MAL6 locus has previously been shown to contain a regulatory gene, the MAL6 locus must be a complex locus containing at least two of the factors needed for maltose fermentation: the structural gene for maltase and the maltase regulatory protein. The absence of other fragments which hybridize to the MAL6 -derived probe shows that either MAL2 and MAL4 are not related to MAL6 , or the DNA corresponding to these genes is absent from the MAL6 strain CB11.

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Repeated Family of Genes Controlling Maltose Fermentation inSaccharomyces carlsbergensis

Molecular and Cellular Biology ◽

10.1128/mcb.3.5.796 ◽

1983 ◽

Vol 3 (5) ◽

pp. 796-802 ◽

Cited By ~ 19

Author(s):

Richard B. Needleman ◽

Corinne Michels

Keyword(s):

Genetic Analysis ◽

Structural Gene ◽

Regulatory Gene ◽

Regulatory Protein ◽

Physical Analysis ◽

Maltose Permease ◽

Maltose Fermentation ◽

Complex Locus ◽

Dna Fragment

Maltose fermentation inSaccharomycesspp. requires the presence of any one of five unlinked genes:MAL1, MAL2, MAL3, MAL4, orMAL6.Although the genes are functionally equivalent, their natures and relationships to each other are not known. At least three proteins are necessary for maltose fermentation: maltase, maltose permease, and a regulatory protein. TheMALgenes may code for one or more of these proteins. Recently a DNA fragment containing a maltase structural gene has been cloned from aMAL6strain, CB11, to produce plasmid pMAL9-26. We have conducted genetic and physical analyses of strain CB11. The genetic analysis has demonstrated the presence of two crypticMALgenes in CB11,MAL1gandMAL3g(linked toMAL1and toMAL3, respectively), in addition to theMAL6locus. The physical analysis, which used a subclone of plasmid pMAL9-26 as a probe, detected threeHindIII genomic fragments with homology to the probe. Each fragment was shown to be linked to one of theMALloci genetically demonstrated to be present in CB11. Our results indicate that the cloned maltase structural gene in plasmid pMAL9-26 is linked toMAL6.Since theMAL6locus has previously been shown to contain a regulatory gene, theMAL6locus must be a complex locus containing at least two of the factors needed for maltose fermentation: the structural gene for maltase and the maltase regulatory protein. The absence of other fragments which hybridize to theMAL6-derived probe shows that eitherMAL2andMAL4are not related toMAL6, or the DNA corresponding to these genes is absent from theMAL6strain CB11.

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MAL63 codes for a positive regulator of maltose fermentation in Saccharomyces cerevisiae

Current Genetics ◽

10.1007/bf00376740 ◽

1988 ◽

Vol 14 (3) ◽

pp. 201-209 ◽

Cited By ~ 19

Author(s):

Young Sook Change ◽

Robert A. Dubin ◽

Edward Perkins ◽

Doug Forrest ◽

Corinne A. Michels ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Positive Regulator ◽

Maltose Fermentation

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Heterologous expression and functional analysis of the F-box protein Ucc1 from other yeast species in Saccharomyces cerevisiae

Journal of Bioscience and Bioengineering ◽

10.1016/j.jbiosc.2019.06.003 ◽

2019 ◽

Vol 128 (6) ◽

pp. 704-709

Author(s):

Kunio Nakatsukasa ◽

Tomoyuki Kawarasaki ◽

Akihiko Moriyama

Keyword(s):

Saccharomyces Cerevisiae ◽

Functional Analysis ◽

Heterologous Expression ◽

Yeast Species ◽

F Box Protein

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Functional analysis of Rpn4-like proteins from Komagataella (Pichia) pastoris and Yarrowia lipolytica on a genetic background of Saccharomyces cerevisiae

Applied Biochemistry and Microbiology ◽

10.1134/s0003683815070029 ◽

2015 ◽

Vol 51 (7) ◽

pp. 757-765

Author(s):

E. N. Grineva ◽

A. T. Leinsoo ◽

D. S. Spasskaya ◽

D. S. Karpov ◽

V. L. Karpov

Keyword(s):

Saccharomyces Cerevisiae ◽

Functional Analysis ◽

Pichia Pastoris ◽

Yarrowia Lipolytica ◽

Genetic Background

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Screening for Theileria parva secretory gene products by functional analysis in Saccharomyces cerevisiae

Molecular and Biochemical Parasitology ◽

10.1016/s0166-6851(00)00236-x ◽

2000 ◽

Vol 109 (1) ◽

pp. 81-87 ◽

Cited By ~ 7

Author(s):

Susan Musembi ◽

Rozmin Janoo ◽

Bali Sohanpal ◽

Horace Ochanda ◽

Onesmo ole-MoiYoi ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Functional Analysis ◽

Gene Products ◽

Theileria Parva

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Functional analysis of human aromatic amino acid transporter MCT10/TAT1 using the yeast Saccharomyces cerevisiae

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/j.bbamem.2017.07.013 ◽

2017 ◽

Vol 1859 (10) ◽

pp. 2076-2085 ◽

Cited By ~ 11

Author(s):

Satoshi Uemura ◽

Takahiro Mochizuki ◽

Goyu Kurosaka ◽

Takanori Hashimoto ◽

Yuki Masukawa ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Functional Analysis ◽

Amino Acid ◽

Aromatic Amino Acid ◽

Amino Acid Transporter ◽

Yeast Saccharomyces Cerevisiae ◽

Acid Transporter

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Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae

Human Molecular Genetics ◽

10.1093/hmg/10.18.1889 ◽

2001 ◽

Vol 10 (18) ◽

pp. 1889-1900 ◽

Cited By ~ 45

Author(s):

A. R. Ellison

Keyword(s):

Saccharomyces Cerevisiae ◽

Functional Analysis ◽

Missense Variants

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Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae

International Journal of Molecular Sciences ◽

10.3390/ijms21238938 ◽

2020 ◽

Vol 21 (23) ◽

pp. 8938

Author(s):

Sebastian Piłsyk ◽

Urszula Perlinska-Lenart ◽

Anna Janik ◽

Elżbieta Gryz ◽

Marta Ajchler-Adamska ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Functional Analysis ◽

Trichoderma Reesei ◽

Transmembrane Domain ◽

Human Cells ◽

Catalytic Subunit ◽

Yeast Saccharomyces Cerevisiae ◽

Dolichyl Phosphate ◽

Functional Homolog ◽

Wide Range

In a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast Saccharomyces cerevisiae, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in S. cerevisiae by the C-terminal transmembrane domain of the catalytic subunit Dpm1. Until present, the regulatory Dpm2 protein has not been found in S. cerevisiae. In this study, we show that, in fact, the Yil102c-A protein interacts directly with Dpm1 in S. cerevisiae and influences its DPM synthase activity. Deletion of the YIL102c-A gene is lethal, and this phenotype is reversed by the dpm2 gene from Trichoderma reesei. Functional analysis of Yil102c-A revealed that it also interacts with glucosylphosphatidylinositol-N-acetylglucosaminyl transferase (GPI-GnT), similar to DPM2 in human cells. Taken together, these results show that Yil102c-A is a functional homolog of DPMII from T. reesei and DPM2 from humans.

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