FACULTY

Gabor Mocz, PhD
Associate Professor
Head, Microarray Core Facility
APITMID Technical Core

Research interests: My primary research interest is in the unraveling of the molecular structures and mechanisms that underlie the beating movement of cilia and flagella. Ciliary and flagellar bending depends on the interaction of dynein, a mechanochemical ATPase with tubulin, a structural subunit of the microtubule skeleton of cilia and flagella. Dynein is one of the largest enzyme known, structurally distinct from other mechanochemical ATPases: the myosins and the kinesins. My work is focused on the substructure of sea urchin axonemal dynein and the relation of its domains to functionally important ATP-binding and tubulin-binding sites with a view to produce insight into normal and pathological processes that involve dynein-mediated motility. Over the years, I probed structural features, regions of interaction and functionally related conformational changes by a variety of biochemical techniques as well as fluorescence and circular dichroic spectroscopy in combination with limited enzymatic proteolysis and photocatalytic peptide cleavage. I was also involved in molecular cloning and sequence analysis of the dynein beta heavy chain. The deduced sequence revealed the existence of multiple nucleotide-binding sites which I subsequently probed by phase partition analysis and fluorescence anisotropy titrations. The sites could be characterized as non-hydrolytic regulatory binding sites that represent an as yet unknown functional aspect of the dynein heavy chain. Most recently, I am working on macromolecular modeling of the three-dimensional structure of the dynein ATP-binding sites. The existence of a distant but highly significant similarity with a recently recognized group of AAA+ ATPases may well constitute a common structural and evolutive nucleus for the nucleotide binding domains of dynein and its putative non-mechanochemical relatives. The models will provide structural clues on how ATP-hydrolysis can be used to produce ciliary and flagellar bendig, and how dyneins may share distinct structural and mechanistic features with members of the AAA+ superfamily of ATPases.

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