User:Emily Leiderman/Sandbox 1

Introduction

The reversible acetylation of lysine residues of histone has been proven to play an important role in the regulation of heterochromatin (inactive) and euchromatin (active). The role of the protein Histone Acetyltransferase is to transfer an acetyl group from to a lysine group found on a histone. This results in an increase in gene activity as the addition of acetyl groups to histones results in the formation of euchromatin. In this study we analyzed the structure and function of the HAT1 gene that’s derived from Saccharomyces cerevisiae. Analysis of the various binding sites and interaction mechanisms involved in the acetylation process in addition to the initial Acetyl CoA binding mechanism ^[1] .

Structure

The structure of HATs consist of a with at least 3 stranded antiparallel β-sheets and one α-helix spanning the length of the sheet. Specifically, Hat1 has an elongated and curved structure that is comprised of 320 residues. The elongated shape of Hat1 allows for the formation of a concave surface where Acetyl CoA binds to the protein.

Domains

It is composed of a mixture of helices and sheets that form two domains. The domains are connected via an extended loop region that together make up the quaternary structure of the protein. The stretches from residues 2-111 and the extends from residues 122-320. Residues 112–121 are what are thought to construct the extended loop that connects the two domains. Additionally, the C-terminal domain contains the active site.

Active Site

Hydrophobic Pocket

Mechanism

Protein Gate

Homology to Other Proteins

References

Student Contributors