<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chen, Linan</style></author><author><style face="normal" font="default" size="100%">Lopes, John M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae.</style></title><secondary-title><style face="normal" font="default" size="100%">Yeast</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Yeast</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Basic Helix-Loop-Helix Leucine Zipper Transcription Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Basic Helix-Loop-Helix Transcription Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Citrate (si)-Synthase</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Enzymologic</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Fungal</style></keyword><keyword><style  face="normal" font="default" size="100%">Inositol</style></keyword><keyword><style  face="normal" font="default" size="100%">Regulatory Sequences, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Saccharomyces cerevisiae</style></keyword><keyword><style  face="normal" font="default" size="100%">Saccharomyces cerevisiae Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">345-59</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The basic helix-loop-helix (bHLH) proteins comprise a eukaryotic transcription factor family involved in multiple biological processes. They have the ability to form multiple dimer combinations and most of them also bind a 6 bp site (E-box) with limited specificity. These properties make them ideal for combinatorial regulation of gene expression. The Saccharomyces cerevisiae CIT2 gene, which encodes citrate synthase, was previously known to be induced by the bHLH proteins Rtg1p and Rtg3p in response to mitochondrial damage. Rtg1p-Rtg3p dimers bind two R-boxes (modified E-boxes) in the CIT2 promoter. The current study tested the ability of all nine S. cerevisiae bHLH proteins to regulate the CIT2 gene. The results showed that expression of CIT2-lacZ reporter was induced in a rho(0) strain by the presence of inositol via the Ino2p and Ino4p bHLH proteins, which are known regulators of phospholipid synthesis. Promoter mutations revealed that inositol induction required a distal E-box in the CIT2 promoter. Interestingly, deleting the INO2, INO4 genes or the cognate E-box revealed phosphate induction of CIT2 expression. This layer of expression required the two R-boxes and the Pho4p bHLH protein, which is known to be required for phosphate-specific regulation. Lastly, the data show that the Hms1p and Sgc1p bHLH proteins also play important roles in repression of CIT2-lacZ expression. Collectively, these results support the model that yeast bHLH proteins coordinate different biological pathways.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chen, Meng</style></author><author><style face="normal" font="default" size="100%">Hancock, Leandria C</style></author><author><style face="normal" font="default" size="100%">Lopes, John M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Transcriptional regulation of yeast phospholipid biosynthetic genes.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochim Biophys Acta</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochim. Biophys. Acta</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase</style></keyword><keyword><style  face="normal" font="default" size="100%">Fungal Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Enzymologic</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Fungal</style></keyword><keyword><style  face="normal" font="default" size="100%">Intramolecular Lyases</style></keyword><keyword><style  face="normal" font="default" size="100%">Myo-Inositol-1-Phosphate Synthase</style></keyword><keyword><style  face="normal" font="default" size="100%">Phospholipids</style></keyword><keyword><style  face="normal" font="default" size="100%">Saccharomyces cerevisiae Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Yeasts</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2007 Mar</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1771</style></volume><pages><style face="normal" font="default" size="100%">310-21</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The last several years have been witness to significant developments in understanding transcriptional regulation of the yeast phospholipid structural genes. The response of most phospholipid structural genes to inositol is now understood on a mechanistic level. The roles of specific activators and repressors are also well established. The knowledge of specific regulatory factors that bind the promoters of phospholipid structural genes serves as a foundation for understanding the role of chromatin modification complexes. Collectively, these findings present a complex picture for transcriptional regulation of the phospholipid biosynthetic genes. The INO1 gene is an ideal example of the complexity of transcriptional control and continues to serve as a model for studying transcription in general. Furthermore, transcription of the regulatory genes is also subject to complex and essential regulation. In addition, databases resulting from a plethora of genome-wide studies have identified regulatory signals that control one of the essential phospholipid biosynthetic genes, PIS1. These databases also provide significant clues for other regulatory signals that may affect phospholipid biosynthesis. Here, we have tried to present a complete summary of the transcription factors and mechanisms that regulate the phospholipid biosynthetic genes.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16854618?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adams, M W</style></author><author><style face="normal" font="default" size="100%">Holden, J F</style></author><author><style face="normal" font="default" size="100%">Menon, A L</style></author><author><style face="normal" font="default" size="100%">Schut, G J</style></author><author><style face="normal" font="default" size="100%">Grunden, A M</style></author><author><style face="normal" font="default" size="100%">Hou, C</style></author><author><style face="normal" font="default" size="100%">Hutchins, A M</style></author><author><style face="normal" font="default" size="100%">Jenney, F E</style></author><author><style face="normal" font="default" size="100%">Kim, C</style></author><author><style face="normal" font="default" size="100%">Ma, K</style></author><author><style face="normal" font="default" size="100%">Pan, G</style></author><author><style face="normal" font="default" size="100%">Roy, R</style></author><author><style face="normal" font="default" size="100%">Sapra, R</style></author><author><style face="normal" font="default" size="100%">Story, S V</style></author><author><style face="normal" font="default" size="100%">Verhagen, M F</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus.</style></title><secondary-title><style face="normal" font="default" size="100%">J Bacteriol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Bacteriol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Culture Media</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoplasm</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Archaeal</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Enzymologic</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Pyrococcus furiosus</style></keyword><keyword><style  face="normal" font="default" size="100%">Sulfur</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 Jan</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">183</style></volume><pages><style face="normal" font="default" size="100%">716-24</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The hyperthermophilic archaeon Pyrococcus furiosus grows optimally at 100 degrees C by the fermentation of peptides and carbohydrates. Growth of the organism was examined in media containing either maltose, peptides (hydrolyzed casein), or both as the carbon source(s), each with and without elemental sulfur (S(0)). Growth rates were highest on media containing peptides and S(0), with or without maltose. Growth did not occur on the peptide medium without S(0). S(0) had no effect on growth rates in the maltose medium in the absence of peptides. Phenylacetate production rates (from phenylalanine fermentation) from cells grown in the peptide medium containing S(0) with or without maltose were the same, suggesting that S(0) is required for peptide utilization. The activities of 14 of 21 enzymes involved in or related to the fermentation pathways of P. furiosus were shown to be regulated under the five different growth conditions studied. The presence of S(0) in the growth media resulted in decreases in specific activities of two cytoplasmic hydrogenases (I and II) and of a membrane-bound hydrogenase, each by an order of magnitude. The primary S(0)-reducing enzyme in this organism and the mechanism of the S(0) dependence of peptide metabolism are not known. This study provides the first evidence for a highly regulated fermentation-based metabolism in P. furiosus and a significant regulatory role for elemental sulfur or its metabolites.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11133967?dopt=Abstract</style></custom1></record></records></xml>