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SPT3 Spt3p

SPT3, Spt3p
The SPTLC3 gene encodes an isoform of the third subunit of serine palmitoyltransferase (SPT; EC, which catalyzes the rate-limiting step of the de novo synthesis of sphingolipids (Hornemann et al., 2006 [PubMed 17023427]). SPT contains 2 main subunits: the common SPTLC1 subunit (MIM 605712) and either SPTLC2 (MIM 605713) or its isoform SPTLC2L (SPTLC3), depending on the tissue in which biosynthesis occurs (Hornemann et al., 2006 [PubMed 17023427]). There are also 2 highly related isoforms of a third subunit, SSSPTA (MIM 613540) and SSSPTB (MIM 610412), that confer acyl-CoA preference of the SPT enzyme and are essential for maximal enzyme activity (Han et al., 2009 [PubMed 19416851]).[supplied by OMIM, Nov 2010] (from NCBI)
Top mentioned proteins: TBP, Histone, CAN, POLYMERASE, TAF
Papers on SPT3
SGF29 and Sry pathway in hepatocarcinogenesis.
Tashiro et al., Hamamatsu, Japan. In World J Biol Chem, Sep 2015
Here, we discuss the molecular nature of SFG29 in SPT3-TAF9-GCN5-acetyltransferase complex, a counterpart of yeast SAGA complex, and the mechanism through which the elevated SGF29 expression contribute to oncogenic potential of c-Myc in hepatocellularcarcinoma (HCC).
Transcription factors spt3 and spt8 are associated with conidiation, mycelium growth, and pathogenicity in Fusarium graminearum.
Zhou et al., Nanjing, China. In Fems Microbiol Lett, 2014
The transcription factors spt3 and spt8 are components of the SAGA complex and they are important in yeasts and filamentous fungi including F. graminearum.
GCN5 acetylates and regulates the stability of the oncoprotein E2A-PBX1 in acute lymphoblastic leukemia.
Wallberg et al., Stockholm, Sweden. In Leukemia, 2013
In the current work we report, for the first time, a physical and functional interaction between the SPT3-TAFII31-GCN5L acetylase (STAGA) complex and E2A-PBX1.
SAGA complex components and acetate repression in Aspergillus nidulans.
Kelly et al., Adelaide, Australia. In G3 (bethesda), 2012
We also made mutations in sptC, homologous to the yeast SAGA component gene SPT3, which showed a similar phenotype.
Increased ethanol production from glycerol by Saccharomyces cerevisiae strains with enhanced stress tolerance from the overexpression of SAGA complex components.
Han et al., Seoul, South Korea. In Enzyme Microb Technol, 2012
To increase ethanol production from glycerol, a greater tolerance to osmotic and ethanol stress was engineered in yeast strains that were impaired in endogenous glycerol production by the overexpression of both SPT3 and SPT15, components of the SAGA (Spt-Ada-Gcn5-acetyltransferase) complex.
Adaptive evolution of loci covarying with the human African Pygmy phenotype.
Comas et al., Barcelona, Spain. In Hum Genet, 2012
identified a significant excess of genes with pivotal roles in bone homeostasis, such as PPPT3B and the height associated SUPT3H-RUNX2
Identification of pathogenesis-associated genes by T-DNA-mediated insertional mutagenesis in Botrytis cinerea: a type 2A phosphoprotein phosphatase and an SPT3 transcription factor have significant impact on virulence.
Tudzynski et al., Münster, Germany. In Mol Plant Microbe Interact, 2012
Two T-DNA integration events that were found to be linked to virulence were characterized in more detail: a catalytic subunit of a PP2A serine/threonine protein phosphatase (BcPP2Ac) and the SPT3 subunit of a Spt-Ada-Gcn5-acetyltransferase (SAGA-like) transcriptional regulator complex.
Ataxin-7 associates with microtubules and stabilizes the cytoskeletal network.
Okazawa et al., Tokyo, Japan. In Hum Mol Genet, 2012
The spinocerebellar ataxia type 7 (SCA7) gene product, Ataxin-7 (ATXN7), localizes to the nucleus and has been shown to function as a component of the TATA-binding protein-free TAF-containing-SPT3-TAF9-GCN5-acetyltransferase transcription complex, although cytoplasmic localization of ATXN7 in affected neurons of human SCA7 patients has also been detected.
[Improving ethanol tolerance of Saccharomyces cerevisiae industrial strain by directed evolution of SPT3].
Bai et al., Dalian, China. In Sheng Wu Gong Cheng Xue Bao, 2010
In this study, we used error-prone PCR for the directed evolution of SPT3, which is the component of yeast Spt-Ada-Gcn5-acetyltransferase (SAGA) complex responsible for the transcription of stress-related genes, and studied its effect on the improvement of ethanol tolerance.
Snf1p regulates Gcn5p transcriptional activity by antagonizing Spt3p.
Kuo et al., East Lansing, United States. In Genetics, 2010
Gcn5p is a target regulated by the competing actions of Snf1p and Spt3p.
SAGA and Rpd3 chromatin modification complexes dynamically regulate heat shock gene structure and expression.
Gross et al., Shreveport, United States. In J Biol Chem, 2009
SAGA and Rpd3 complexes are rapidly and synchronously recruited to heat shock factor 1-activated genes
The SPTLC3 subunit of serine palmitoyltransferase generates short chain sphingoid bases.
von Eckardstein et al., Zürich, Switzerland. In J Biol Chem, 2009
Data show that the SPTLC3 subunit generates C(16)-sphingoid bases and that sphingolipids with a C(16) backbone constitute a significant proportion of plasma sphingolipids.
Effect of overexpression of transcription factors on the fermentation properties of Saccharomyces cerevisiae industrial strains.
Lu et al., Tianjin, China. In Lett Appl Microbiol, 2009
Simultaneous modulation of the expression level of SPT15 and SPT3 can increase the production of ethanol by improving osmotic tolerance and ethanol tolerance of industrial strains.
Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein.
Martinez et al., Riverside, United States. In J Biol Chem, 2009
In contrast, vertebrate organisms, express two paralogous GCN5-like acetyltransferases (GCN5 and PCAF), which have been found so far only in SAGA-type complexes referred to hereafter as the STAGA (SPT3-TAF9-GCN5/PCAF acetylase) complexes.
Characterization of new Spt3 and TATA-binding protein mutants of Saccharomyces cerevisiae: Spt3 TBP allele-specific interactions and bypass of Spt8.
Winston et al., Boston, United States. In Genetics, 2007
a direct Spt3-TATA-binding protein interaction is required for normal TATA-binding protein levels at Spt3-dependent promoters in vivo.
Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation.
Tora et al., France. In Oncogene, 2007
Metazoan GCN5 and PCAF are subunits of at least two types of multiprotein complexes, one having a molecular weight of 2 MDa (SPT3-TAF9-GCN5 acetyl transferase/TATA binding protein (TBP)-free-TAF complex/PCAF complexes) and a second type with about a size of 700 kDa (ATAC complex).
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.
Moras et al., Strasbourg, France. In Cell, 1998
The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions.
The SPT3 gene is required for normal transcription of Ty elements in S. cerevisiae.
Fink et al., In Cell, 1984
Mutations in the SPT3 gene suppress these effects of Ty and delta insertion mutations on adjacent genes.
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