About Us

The Armache lab is interested in understanding the mechanisms and functions of ATP-dependent chromatin remodeling complexes and their place in genome regulation. The genome in eukaryotes is organized into chromatin, a condensed superstructure that evolved to keep DNA protected from damage and to tightly control gene expression. The basic unit of chromatin is the nucleosome, an octamer of proteins called histones wrapped by DNA. Cells evolved chromatin regulators to control critical steps in development and differentiation through processes such as DNA methylation, post-translational histone modifications, ATP-dependent remodeling, and mechanisms that establish a specific chromatin state. To this end, histones contain elongated tails that can be post-translationally modified. This is established, maintained, and interpreted mainly by non-histone chromosomal proteins. In turn, ATP-dependent chromatin remodelers modulate DNA accessibility by repositioning DNA with respect to the histones using energy from ATP hydrolysis. These macromolecular machines are employed and influence a range of processes, such as transcription, replication and repair.

To maintain or effectuate changes in chromatin, eukaryotic cells evolved several different families of ATP-dependent remodeling factors: SWI/SNF/, ISWI, Ino80 and CHD, that possess their own unique properties. They all share the ATPase core, but contain additional domains that affect their functionalities, behavior or time at which they are activated. These complexes can contain just a single ATP-ase or can employ additional accessory subunits that change their targeting and behavior. In the Armache lab, we are interested in structural and mechanistic studies of ATP-dependent chromatin remodeling complexes that are associated with human diseases. We probe the structures using a range of biochemical and biophysical approaches, using cryo-electron microscopy (cryo-EM) for structural determination. At the same time, we also extend our techniques to a number of membrane protein targets that are relevant in human diseases. We are also interested in pushing forward the technology in electron microscopy, hoping that our efforts will increase the adoption and decrease the amount of training required by scientists to use cryo-EM.

I joined Penn State University in April 2019 as a faculty at the Department of Biochemistry and Molecular Biology, Eberly College and the Huck Institutes of Life Sciences. I obtained my PhD in 2011 at the Ludwig-Maximilians-University in Munich, Germany. Subsequently, I left Europe for California to join University of California San Francisco as a postdoctoral scholar. Originally from Poland, I graduated as MSc in 2006 from the Technical University of Lodz in Computer Science.