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Transcription elongation regulator 1

CA150, FBP28, TCERG1
This gene encodes a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. The encoded protein interacts with the hyperphosphorylated C-terminal domain of RNA polymerase II via multiple FF domains, and with the pre-mRNA splicing factor SF1 via a WW domain. Alternative splicing results in multiple transcripts variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, POLYMERASE, ACID, AGE, SF-1
Papers on CA150
Binding of Cu(II) ions to peptides studied by fluorescence spectroscopy and isothermal titration calorimetry.
Chmurzyński et al., Gdańsk, Poland. In Spectrochim Acta A Mol Biomol Spectrosc, Feb 2016
Two of them were taken from the N-terminal part of the FBP28 protein (formin binding protein) WW domain: Tyr-Lys-Thr-Ala-Asp-Gly-Lys-Thr-Tyr-NH2 (D9) and its mutant Tyr-Lys-Thr-Ala-Asn-Gly-Lys-Thr-Tyr-NH2 (D9_M) as well as two mutated peptides from the B3 domain of the immunoglobulin binding protein G derived from Streptococcus: Asp-Val-Ala-Thr-Tyr-Thr-NH2 (J1) and Glu-Val-Ala-Thr-Tyr-Thr-NH2 (J2).
Preventing fibril formation of a protein by selective mutation.
Scheraga et al., Barcelona, Spain. In Proc Natl Acad Sci U S A, Dec 2015
The origins of formation of an intermediate state involved in amyloid formation and ways to prevent it are illustrated with the example of the Formin binding protein 28 (FBP28) WW domain, which folds with biphasic kinetics.
The Glutamine-Alanine Repeat Domain of TCERG1 is Required for the Inhibition of the Growth Arrest Activity of C/EBPα.
Roesler et al., Saskatoon, Canada. In J Cell Biochem, Sep 2015
UNASSIGNED: TCERG1 was characterized previously as a repressor of the transcription factor C/EBPα through a mechanism that involved relocalization of TCERG1 from nuclear speckles to pericentromeric regions.
A study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamics.
Chmurzyński et al., Gdańsk, Poland. In Protein J, 2014
The β-hairpins of FBP28 WW domain and IgG are stable and have been proved to initiate the folding and are, therefore, suitable for studying the influence of charged residues on β-hairpin conformation.
Germline signals deploy NHR-49 to modulate fatty-acid β-oxidation and desaturation in somatic tissues of C. elegans.
Ghazi et al., San Francisco, United States. In Plos Genet, 2014
Following germline ablation, NHR-49 is up-regulated in somatic cells by the conserved longevity determinants DAF-16/FOXO and TCER-1/TCERG1.
Functional Consequences for Apoptosis by Transcription Elongation Regulator 1 (TCERG1)-Mediated Bcl-x and Fas/CD95 Alternative Splicing.
Suñé et al., Granada, Spain. In Plos One, 2014
Here, we present evidence for a specific role of the splicing-related factor TCERG1 in regulating apoptosis in live cells by modulating the alternative splicing of the apoptotic genes Bcl-x and Fas.
A new optimized formulation of cationic solid lipid nanoparticles intended for gene delivery: development, characterization and DNA binding efficiency of TCERG1 expression plasmid.
Miñarro et al., Barcelona, Spain. In Int J Pharm, 2014
The suitability of the optimized SLNs for DNA binding was evaluated after the lyophilisation process using a carboxyl-terminal region of the TCERG1 gene, a human factor that has been implicated in several diseases.
WW domain folding complexity revealed by infrared spectroscopy.
Dyer et al., Atlanta, United States. In Biochemistry, 2014
Here we demonstrate the advantages of using multiple probes, infrared and fluorescence spectroscopy, to study the folding of the FBP28 WW domain.
Dynamics of an ultrafast folding subdomain in the context of a larger protein fold.
Dyer et al., Atlanta, United States. In J Am Chem Soc, 2014
The folding of the wild type FBP28 WW domain was compared to constructs in which each of the loops was replaced by CLN025.
Functional characterization of duplicated Suppressor of Overexpression of Constans 1-like genes in petunia.
Jha et al., Burlington, United States. In Plos One, 2013
Furthermore, expression levels of the SOC1-like genes Unshaven (UNS) and Floral Binding Protein 21 (FBP21), but not FBP28, are positively correlated with developmental age.
Local vs global motions in protein folding.
Scheraga et al., Ithaca, United States. In J Chem Theory Comput, 2013
This question is addressed by analyzing folding and non-folding trajectories of a protein; as an example, the analysis is applied to the 37-residue triple β-strand WW domain from the Formin binding protein 28 (FBP28) (PDB ID: 1E0L).
Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.
Zhou et al., Durham, United States. In J Biol Chem, 2013
The human transcription elongation regulator TCERG1 physically couples transcription elongation and splicing events by interacting with splicing factors through its N-terminal WW domains and the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II through its C-terminal FF domains.
Transcriptional networks that mediate signals from reproductive tissues to influence lifespan.
Ghazi, Pittsburgh, United States. In Genesis, 2013
This network includes conserved, longevity-promoting Forkhead Box (FOX) family transcription factors such as DAF-16/FOXO and PHA-4/FOXA, nuclear hormone receptors, as well as a transcription elongation factor, TCER-1/TCERG1.
Transcription elongation regulator 1 (TCERG1) regulates competent RNA polymerase II-mediated elongation of HIV-1 transcription and facilitates efficient viral replication.
Suñé et al., Granada, Spain. In Retrovirology, 2012
Here, we present evidence for a specific role of the elongation-related factor TCERG1 in regulating the extent of HIV-1 elongation and viral replication in vivo.
The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.
Suñé et al., Armilla, Spain. In J Biol Chem, 2012
The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.
TCERG1 regulates alternative splicing of the Bcl-x gene by modulating the rate of RNA polymerase II transcription.
Suñé et al., Granada, Spain. In Mol Cell Biol, 2012
We propose that TCERG1 modulates the elongation rate of RNAPII to relieve pausing, thereby activating the proapoptotic Bcl-x(S) 5' splice site.
TCERG1 inhibits C/EBPα through a mechanism that does not involve sequestration of C/EBPα at pericentromeric heterochromatin.
Roesler et al., Saskatoon, Canada. In J Cell Biochem, 2011
TCERG1 can inhibit C/EBPalpha activity regardless of the latter's location in the nucleus
The ensemble folding kinetics of the FBP28 WW domain revealed by an all-atom Monte Carlo simulation in a knowledge-based potential.
Shakhnovich et al., Cambridge, United States. In Proteins, 2011
The study examines the order of formation of two beta-hairpins, the folding mechanism of each individual beta-hairpin, and transition state ensemble of formin-binding protein 28, FBP28 WW domain.
Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1).
Suñé et al., Granada, Spain. In J Biol Chem, 2010
mutation of the SUMO acceptor lysine residues enhanced TCERG1 transcriptional activity, indicating that SUMO modification negatively regulates TCERG1 transcriptional activity
Force Field Effects on a β-Sheet Protein Domain Structure in Thermal Unfolding Simulations.
Wade et al., Heidelberg, Germany. In J Chem Theory Comput, 2006
Motivated by thermal unfolding simulations of several WW domains, which have a three-stranded β-sheet structure, we chose the FBP28 WW domain as a well-characterized system to investigate several AMBER force fields as well as parametrization of the NPSA (Neutralized, Polarized ionizable side chains with a solvent-accessible Surface Area-dependent term) implicit solvent model.
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