Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-12-12
pubmed:abstractText
The filamentous fungi Aspergillus nidulans and Neurospora crassa and the yeast Saccharomyces cerevisiae each possess a global regulatory circuit that controls the expression of permeases and enzymes that function both in the acquisition of sulfur from the environment and in its assimilation. Control of the structural genes that specify an array of enzymes that catalyze reactions of sulfur metabolism occurs at the transcriptional level and involves both positive-acting and negative-acting regulatory factors. Positive trans-acting regulatory proteins that contain a basic region, leucine zipper-DNA binding domain, are found in Neurospora and yeast. Each of these fungi contain a sulfur regulatory protein of the beta-transducin family that acts in a negative fashion to control gene expression. Sulfur regulation in yeast also involves the general DNA binding protein, centromere binding factor I. Sulfate uptake is a highly regulated step and appears to occur in fungi, plants, and mammals via a family of related transporter proteins. Recent developments have provided new insight into the nature and control of the enzymes ATP sulfurylase and APS kinase, which catalyze the early steps of sulfate assimilation, and of the Aspergillus enzyme, cysteine synthase, which produces cysteine from O-acetylserine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Anion Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/CYS3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Cystathionine gamma-Lyase, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sulfate Adenylyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Sulfates, http://linkedlifedata.com/resource/pubmed/chemical/Sulfur, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/adenylylsulfate kinase, http://linkedlifedata.com/resource/pubmed/chemical/sulfate permease
pubmed:status
MEDLINE
pubmed:issn
0066-4227
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
73-96
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9343344-Anion Transport Proteins, pubmed-meshheading:9343344-Aspergillus nidulans, pubmed-meshheading:9343344-Cystathionine gamma-Lyase, pubmed-meshheading:9343344-Cysteine, pubmed-meshheading:9343344-DNA-Binding Proteins, pubmed-meshheading:9343344-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9343344-Gene Expression Regulation, Fungal, pubmed-meshheading:9343344-Membrane Transport Proteins, pubmed-meshheading:9343344-Neurospora crassa, pubmed-meshheading:9343344-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:9343344-Saccharomyces cerevisiae, pubmed-meshheading:9343344-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9343344-Sulfate Adenylyltransferase, pubmed-meshheading:9343344-Sulfates, pubmed-meshheading:9343344-Sulfur, pubmed-meshheading:9343344-Transcription Factors
pubmed:year
1997
pubmed:articleTitle
Molecular genetics of sulfur assimilation in filamentous fungi and yeast.
pubmed:affiliation
Department of Biochemistry and Program in Molecular, Cellular, and Developmental Biology, The Ohio State University, Columbus 43210, USA. marzluf.1@osu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review