scholarly journals Identification of Amino Acid Residues in the ETS Transcription Factor Erg That Mediate Erg-Jun/Fos-DNA Ternary Complex Formation

2001 ◽  
Vol 276 (20) ◽  
pp. 17181-17189 ◽  
Author(s):  
Alexis Verger ◽  
Eric Buisine ◽  
Séverine Carrère ◽  
René Wintjens ◽  
Anne Flourens ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Complex Formation ◽  
Ternary Complex ◽  
Amino Acid Residues ◽  
Ternary Complex Formation ◽  
Ets Transcription Factor

Evidence for albumin – Cu(II) – amino acid ternary complex

1968 ◽  
Vol 46 (6) ◽  
pp. 601-607 ◽  
Author(s):  
Bibudhendra Sarkar ◽  
Yuk Wigfield
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Complex Formation ◽  
Binding Sites ◽  
Ternary Complex ◽  
Binding Studies ◽  
Acid Complex ◽  
Ternary Complex Formation ◽  
Chelex 100 ◽  
Amino Acid Complex

Commercially obtained pure human serum albumin (HSA) was shown to contain molecular aggregates and was significantly contaminated with Cu(II). A solution of commercial HSA was first passed through a Sephadex G-200 column to obtain pure monomeric HSA. The monomer of HSA was subsequently passed through Chelex-100 resin to free it from Cu(II). All Cu(II)-binding studies were conducted with monomeric and copper-free HSA. The first Cu(II)-binding site on HSA appears to be stronger than the second and the subsequent binding sites. Significant amounts of L-histidine and L-threonine were bound to HSA when Cu(II) was added in the form of Cu(II) – amino acid complexes. In the absence of Cu(II), free L-histidine or L-threonine do not bind to HSA at pH 7.4. It is concluded that, in the presence of either L-histidine or L-threonine, ternary complex formation is involved both at the first and the subsequent binding sites for Cu(II) on HSA. In view of this finding, it appears that the equilibrium between HSA–Cu(II) and Cu(II) – amino acid complex is mediated through a ternary complex HSA – Cu(II) – amino acid.

scholarly journals The acute transcriptional responses to dietary methionine restriction are triggered by inhibition of ternary complex formation and linked to Erk1/2, mTOR, and ATF4

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Kirsten P. Stone ◽  
Sujoy Ghosh ◽  
Jean Paul Kovalik ◽  
Manda Orgeron ◽  
Desiree Wanders ◽  
...  
Keyword(s):  
Stress Response ◽  
Complex Formation ◽  
Ternary Complex ◽  
Target Genes ◽  
Bioinformatic Analysis ◽  
Transcriptional Responses ◽  
Metabolomics Data ◽  
Ternary Complex Formation ◽  
Methionine Restriction

AbstractThe initial sensing of dietary methionine restriction (MR) occurs in the liver where it activates an integrated stress response (ISR) that quickly reduces methionine utilization. The ISR program is regulated in part by ATF4, but ATF4’s prototypical upstream regulator, eIF2α, is not acutely activated by MR. Bioinformatic analysis of RNAseq and metabolomics data from liver samples harvested 3 h and 6 h after initiating MR shows that general translation is inhibited at the level of ternary complex formation by an acute 50% reduction of hepatic methionine that limits formation of initiator methionine tRNA. The resulting ISR is induced by selective expression of ATF4 target genes that mediate adaptation to reduced methionine intake and return hepatic methionine to control levels within 4 days of starting the diet. Complementary in vitro experiments in HepG2 cells after knockdown of ATF4, or inhibition of mTOR or Erk1/2 support the conclusion that the early induction of genes by MR is partially dependent on ATF4 and regulated by both mTOR and Erk1/2. Taken together, these data show that initiation of dietary MR induces an mTOR- and Erk1/2-dependent stress response that is linked to ATF4 by the sharp, initial drop in hepatic methionine and resulting repression of translation pre-initiation.

Ternary complex formation of the nickel(II), 2,2’-bipyridine, 1,10’-Phenanthroline and some aminoacids

2021 ◽  
pp. 1-11
Author(s):  
Yoselin Jara ◽  
Mary Lorena Araujo ◽  
Waleska Madden ◽  
Vito Lubes ◽  
Lino Hernández
Keyword(s):  
Complex Formation ◽  
Ternary Complex ◽  
Ternary Complex Formation

VPS37 Isoforms Differentially Modulate the Ternary Complex Formation of ALIX, ALG-2, and ESCRT-I

2013 ◽  
Vol 77 (8) ◽  
pp. 1715-1721 ◽  
Author(s):  
Mayumi OKUMURA ◽  
Angela M. KATSUYAMA ◽  
Hideki SHIBATA ◽  
Masatoshi MAKI
Keyword(s):  
Complex Formation ◽  
Ternary Complex ◽  
Ternary Complex Formation
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