DynaMo Mini Symposium: Stefan Binder & Janneke Balk

DynaMo is happy to invite to a Mini Symposium with our two distinguised guests from Germany and the UK respectively.

Programme

10:00
Professor Dr. Stefan Binder, Ulm University, Germany
Dual functions of enzymes involved in the branched-chain amino acid metabolism and in the biosynthesis of methionine-derived aliphatic glucosinolates

11:00
Reader Dr. Janneke Balk, John Innes Centre, UK
The Fe-S connection: what links mitochondria to nuclear genome integrity?

Abstracts

Stefan Binder:

Dual functions of enzymes involved in the branched-chain amino acid metabolism and in the biosynthesis of methionine-derived aliphatic glucosinolates

The presentation focuses on the study of the function of branched-chain aminotransferases and isopropylmalate isomerases in Arabidopsis thaliana. These enzymes are involved in the metabolism of branched-chain amino acids, but some of them are also active in the chain elongation pathway generating methionine derivatives required for the biosynthesis of aliphatic glucosinolates. Recent studies focus on the function of isopropylmalate isomerase small subunit 1, a protein essential of plant viability.

Dr. Stefan Binder is Professor at the Institute for Molecular Botany at the University of Ulm, Germany. His research is centered on RNA-metabolism in mitochondria of higher plants and branched-chain amino acid metabolism. Stefan Binder did his Diploma in Biology at Eberhard Karls University in Tübingen and his PhD degree at the „Institut für Genbiologische Forschung“ in Berlin. From 1992 he worked as a postdoctoral researcher in Berlin until he, in 1995, became research group leader at the at the University of Ulm, Germany. Since 2006 he serves as Apl. Professor at the Institute for Molecular Botany at the University of Ulm.

Janneke Balk:
The Fe-S connection: what links mitochondria to nuclear genome integrity?

Iron is arguably the most widely used metal in biological systems. It is primarily used as cofactor to catalyze enzymatic reactions. Over the past 8 years, we have investigated how iron-sulfur (Fe-S) clusters are assembled in plants and algae. Both mitochondria and plastids have their own assembly pathways of different evolutionary origin. Interestingly, Fe-S proteins in the cytosol and nucleus, including recently discovered proteins in DNA metabolism, depend on the mitochondria. Based on mutant analyses and in-vitro transport studies, we propose that the mitochondria are the source of persulfide (S0) which is exported by a mitochondrial ATP-binding cassette transporter.

Janneke Balk is Reader in Biological Sciences, University of East Anglia and Project Leader at John Innes Centre, Norwich Research Park in the UK. Her research is focussed on the role of metals, in particular iron, in plants and microbes. In the past years, her lab has identified several proteins that are involved in the assembly of iron-sulfur proteins, using the model plant Arabidopsis, the green alga Chlamydomonas and yeasts. Janneke Balk holds an MSc in Cell and Molecular Biology from Wageningen University, Netherlands, and a DPhil. in Biological Sciences from the University of Oxford. During 1999-2002 she was a Junior Research Fellow (E.P. Abraham Cephalosporin) at Lincoln College, Oxford; 2002-2004 she had a Marie Curie post-doctoral fellowship at Philipps-Universität Marburg, Germany; and 2004-2011 she had a Royal Society University Research Fellowship at the University of Cambridge. Since 2011 she joined the University of East Anglia and the John Innes Centre in Norwich.