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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1991-7-17
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D00651,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D00652,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D00653,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D00654,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M38709,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M59448,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63851,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64825,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64826,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64827,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M82963
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pubmed:abstractText |
Two novel genes affecting hexose transport in the yeast Saccharomyces cerevisiae have been identified. The gene HXT1 (hexose transport), isolated from plasmid pSC7, was sequenced and found to encode a hydrophobic protein which is highly homologous to the large family of sugar transporter proteins from eucaryotes and procaryotes. Multicopy expression of the HXT1 gene restored high-affinity glucose transport to the snf3 mutant, which is deficient in a significant proportion of high-affinity glucose transport. HXT1 was unable to complement the snf3 growth defect in low copy number. The HXT1 protein was found to contain 12 putative membrane-spanning domains with a central hydrophilic domain and hydrophilic N- and C-terminal domains. The HXT1 protein is 69% identical to GAL2 and 66% identical to HXT2, and all three proteins were found to have a putative leucine zipper motif at a consensus location in membrane-spanning domain 2. Disruption of the HXT1 gene resulted in loss of a portion of high-affinity glucose and mannose transport, and wild-type levels of transport required both the HXT1 and SNF3 genes. Unexpectedly, expression of beta-galactosidase activity by using a fusion of the lacZ gene to the HXT1 promoter in a multicopy plasmid was maximal during lag and early exponential phases of growth, decreasing approximately 100-fold upon further entry into exponential growth. Deletion analysis of pSC7 revealed the presence of another gene (called ORF2) capable of suppressing the snf3 null mutant phenotype by restoring high-affinity glucose transport and increased low-affinity transport.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-1195397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-1975753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2233722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2653440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2659436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2666404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2689282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2739731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-2985470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3016720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3026915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3053697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3063604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3072253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3273192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3281163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3289117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3319781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3333305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3527041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3540596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3543693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3549699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3839598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-3996185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-5650080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6235151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6300872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6310321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6310323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6310324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6312838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6336730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6350275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-6546423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-7040163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2046678-7108955
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:geneSymbol |
HXT1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3804-13
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2046678-Amino Acid Sequence,
pubmed-meshheading:2046678-Animals,
pubmed-meshheading:2046678-Base Sequence,
pubmed-meshheading:2046678-Cloning, Molecular,
pubmed-meshheading:2046678-DNA, Fungal,
pubmed-meshheading:2046678-Escherichia coli,
pubmed-meshheading:2046678-Genes, Fungal,
pubmed-meshheading:2046678-Genetic Complementation Test,
pubmed-meshheading:2046678-Genotype,
pubmed-meshheading:2046678-Glucose,
pubmed-meshheading:2046678-Hexoses,
pubmed-meshheading:2046678-Kinetics,
pubmed-meshheading:2046678-Molecular Sequence Data,
pubmed-meshheading:2046678-Monosaccharide Transport Proteins,
pubmed-meshheading:2046678-Plasmids,
pubmed-meshheading:2046678-Restriction Mapping,
pubmed-meshheading:2046678-Saccharomyces cerevisiae,
pubmed-meshheading:2046678-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
The HXT1 gene product of Saccharomyces cerevisiae is a new member of the family of hexose transporters.
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pubmed:affiliation |
Department of Viticulture and Enology, University of California, Davis 95616.
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pubmed:publicationType |
Journal Article
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