Ashish Kumar, PhD

I earned my Ph.D. under the guidance of Dr. Dileep Vasudevan at the Institute of Life Sciences, Bhubaneswar, India. Currently, I am working as a postdoctoral associate in the Department of Pharmacology at Yale University under the mentorship of Prof. Joseph Schlessinger.

During my doctoral studies, I spearheaded diverse research projects that centered on the structural and biophysical characterization of plant chromatin and plant-specific histone chaperones. My research endeavors aimed to unravel the intricate mechanisms governing plant chromatin dynamics. Utilizing X-ray Crystallography as my primary investigative tool, in combination with complementary biophysical techniques like SAXS and AUC, I made substantial contributions to our comprehension of plant chromatin regulation, particularly concerning stress-specific histone chaperones of the NRP family and HDT family. Notably, my Ph.D. work led to the discovery that plant HDTs function as histone chaperones within the nucleoplasmin family rather than actively participating in deacetylation.

In my initial postdoctoral role, my research focused on elucidating the mechanisms governing DNA replication initiation in metazoans. Employing an integrative structural biology approach that involved the biochemical reconstitution of nucleosome complexes, mass spectrometry, and cryo-EM, I have co-authored two publications during my tenure at Yale. These studies shed light on how inhibitory signals, such as phosphorylation by cyclin-dependent kinases, can impede DNA replication initiation factor loading. Additionally, we unveiled the pivotal role played by the initiation factor ORC-associated protein, ORCA, in facilitating DNA replication initiation within the context of condensed chromatin. My primary contributions encompassed the preparation of modified histones, nucleosomes, and nucleosome arrays, as well as the execution of various biochemical experiments.

My ongoing research in Prof. Schlessinger's lab centers on solving the cryo-EM structures of receptor tyrosine kinases (RTKs) in complex with their ligands and other signaling molecules.