McHarris, Danielle M.; Barr, Daniel A.
Truncated Variants of the GCN4 Transcription Activator Protein Bind DNA with Dramatically Different Dynamical Motifs
JOURNAL OF CHEMICAL INFORMATION AND MODELING, 54:2869-2875, OCT 2014

The yeast protein GCN4 is a transcriptional activator in the basic leucine zipper (bZip) family, whose distinguishing feature is the "chopstick-like" homodimer of alpha helices formed at the DNA-binding interface. While experiments have shown that truncated versions of the protein retain biologically relevant DNA-binding affinity, we present the results of a computational study revealing that these variants show a wide variety of dynamical modes in their interaction with the target DNA sequence. We have performed all-atom molecular dynamics simulations of the full-length GCN4 protein as well as three truncated variants; our data indicate that the truncated mutants show dramatically different correlation patterns. We conclude that although the truncated mutants still retain DNA-binding ability, the bZip interface present in the full-length protein provides important stability for the protein-DNA complex.

DOI:10.1021/ci500448e

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