Ir. M.H. Hefti : The NifL PAS domain. Insight into its structure and function

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29 Apr 2003 13:30
Unit: Wageningen University
Location: Aula (gebouw 362), Gen. Foulkesweg 1, Wageningen
Promotor: prof.dr. S.C. de Vries (Biochemistry (Molecular Enzymology))
Co Promotor: dr.ir. J. Vervoort

 Azotobacter vinelandii is an aerobic soil-dwelling organism with a wide variety of metabolic capabilities which include the ability to fix atmospheric nitrogen by converting it to ammonia. The biosynthesis of ammonia is controlled by 15 to 20 different nif gene products. The activation of nif gene expression by the regulatory enhancer binding protein NifA is controlled by the sensor flavoprotein NifL in response to changes in oxygen or nitrogen levels. NifL contains a PAS domain, which is an ubiquitous motif present in all kingdoms of life. PAS domains are involved in many regulatory signal transduction processes in a large variety of organisms and they function as on-off switches. In this research the structure and function of this domain has been studied extensively using NMR and X-ray spectroscopy. Comparison of 1000 PAS protein sequences with predicted three dimensional structures resulted in a redefinition of this intriguing sensory domain.
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