Dr. Kristin Baetz

Assistant Professor

Canada Research Chair in Chemical and Functional Genomics

Department of Biochemistry, Microbiology and Immunology Faculty of Medicine, University of Ottawa



Speaker: Dr. Kristin Baetz

Title of the presentation:
A yeast "KATalogue" of genetic and protein interactions identifies novel roles for NuA4 in the cell cycle.

Biography:
B.Sc. Queen's University 1995
Ph.D. University of Toronto 2000
Post-doctoral Research University of British Columbia

Short summary of research interests:
During evolution, there has been a high level of conservation between the budding yeast Saccharomyces cerevisae's cellular processes and those of mammalian cells. The advantages of using S. cerevisiae as a model system are multiple, including easy genetic manipulation and availability of several experimental tools for genetic, biochemical and molecular biology studies. Thus, S. cerevisiae has been the platform model organism for the development of genomic techniques and systems biology to analyze their biological functions. The Baetz laboratory is developing and applying high throughput yeast chemical and functional genomic screening in i) Genetic and Molecular Basis of Chromosome Instability and ii) Identification of Chemical Mode of Action.

Abstract:
Lysine acetyltransferases (KATs) catalyze the transfer of acetyl groups from Acetyl coenzyme A (Acetyl CoA) onto the epsilon amino group of lysines. KAT complexes are highly conserved from yeast to man and have been implicated in a wide variety of diseases from cancer to neurodegenerative disorders. Lysine acetylation was first discovered 40 years ago on histones and in the last decade on transcription factors and important nuclear regulators. However, the dogma that lysine acetylation is limited to histone or chromatin associated proteins has quickly become obsolete. Proteomic "Acetylome" studies from bacteria to man have affinity purified and identified lysine acetylated peptides on a plethora of proteins, from nuclear to secreted proteins. Over 2500 human proteins are already known to be acetylated in vivo, but very few acetylations have been linked to specific KATs. Therefore, to truly understand the role of KATs in disease will require the elucidation of the network of KATs and their substrates (the KATalogue). We have developed a KATalogue for the Saccharomyces cerevisiae KAT complex NuA4 using a multidisciplinary approach that combines yeast functional genomics with a novel mass spectrometry method that simultaneously generates a protein interaction network and can identify both in vivo and in vitro acetylations. Our study has dramatically increased our knowledge of NuA4's cellular functions, non-histone targets and has uncovered novel roles for NuA4 in regulating spindle and septin dynamics, two processes intimately linked with chromosome stability.

 

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