GCN4PDB The Gcn4 transcription factor is a pivotal regulator in yeast, particularly in governing the response to amino acid starvation.作者：M Lu·1999·被引用次数：57—Analytical ultracentrifugation was used to determine the oligomerization states of the mutantpeptides. Over a fourfold range ofpeptideconcentration (150, 300 ... Research into the Gcn4 peptide, specifically its leucine-zipper domain, has been extensive, focusing on its DNA-binding capabilities and structural properties. This peptide plays a crucial role in gene transcription, acting as a master regulator for a significant portion of the yeast genome.
The Gcn4 protein is a conserved eukaryotic basic zipper (bZIP) transcription factor that functions within the general amino acid control (GAAC) network. The Gcn4 peptide, derived from this protein, often refers to specific functional domains, most notably the leucine-zipper region.作者：X Wang·2003·被引用次数：26—Here, for the first time, we present a detailed description of the thermodynamics of a monomericpeptide GCN4-br, the basic region (226–252) ofGCN4, binding to ... This domain is critical for dimerization and DNA binding, enabling the Gcn4 protein to interact with specific DNA target sites. Studies have explored the structure of the Gcn4 leucine zipper, revealing its tendency to form a parallel, two-stranded coiled coil of alpha helices, a characteristic packing arrangement often described by the "knobs-into-holes" model.
The ability of the Gcn4 peptide to bind DNA is a central theme in its research作者：A Iyer·2015·被引用次数：20—The basic DNA recognition region of theGCN4protein comprising 23 amino acids has been modified to contain two optimally positioned .... Modifications to the basic DNA recognition region, comprising approximately 23 amino acids, have been investigated to understand and potentially enhance its DNA-binding affinity and specificity. For instance, research has explored stapling monomeric Gcn4 peptides to achieve specific structural conformations, thereby influencing their interaction with DNA. Furthermore, the reversible photo-cross-linking of Gcn4 peptides, incorporating specific residues like CNVA, has been utilized to study these interactions more dynamically.An Intrahelical Salt Bridge within the Trigger Site Stabilizes ...
The leucine zipper motif within the Gcn4 peptide is a well-characterized structural element. Its formation into coiled coils is essential for the protein's function as a transcription factor.This antibody binds to theGCN4-leucine zipperpeptide, which is part of the dimerisation- and DNA-binding domain of the transcriptional activatorGCN4in S. ... The stability and conformational characteristics of these coiled coils have been a subject of detailed study. For example, the retro-GCN4 leucine zipper sequence has been shown to form a stable, parallel four-helix bundle, offering insights into the underlying principles of protein folding and stability.作者：Z Qiu·2019·被引用次数：8—As a result, it was shown that theGCN4 peptide, containingCNVA, can be photo-cross-linked to DNA, and its adduct was photo-split into the original peptide and ...
Research has also delved into the specific amino acid sequences that contribute to the Gcn4 peptide's function. The presence of histidine and arginine residues within the leucine zipper domains, for instance, has been identified as essential for certain interactions, such as those with RNase A. Studies synthesizing Gcn4 peptides corresponding to specific regions, like the leucine zipper region (amino acids 226-252), have allowed for in-depth analysis of their structural and functional properties. Techniques such as circular dichroism (CD) spectropolarimetry and NMR spectroscopy are frequently employed to characterize these peptides and their interactions.Stapling monomeric GCN4 peptides allows for DNA ...
The Gcn4 peptide and its structural motifs have implications beyond fundamental biological research. Antibodies targeting the Gcn4 leucine-zipper peptide, such as those binding to the HLENEVARLKK sequence, are used as tools in molecular biology research to detect and study the Gcn4 transcriptional activator in *Saccharomyces cerevisiae*2ZTA: X-RAY STRUCTURE OF THE GCN4 LEUCINE ....
Ongoing research continues to explore various aspects of Gcn4 peptides, including their oligomerization states, helix capping within the leucine zipper, and the thermodynamics of their folding and DNA binding. The development of methods for synthesizing and characterizing these peptides, including solid-phase synthesis and modifications for specific experimental purposes, remains a key area of investigation. These studies contribute to a broader understanding of transcription factor function, protein-protein interactions, and the molecular mechanisms governing gene expression in response to cellular stress.作者：X Wang·2003·被引用次数：26—Here, for the first time, we present a detailed description of the thermodynamics of a monomericpeptide GCN4-br, the basic region (226–252) ofGCN4, binding to ...
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