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Forest’s work in this exhibition: Phytochrome, Bacterial Flagellar Base, and ATP Synthase

Phytochrome
Phytochrome is a photoreceptor and a pigment that plants, and some bacteria and fungi, use to detect light. It is sensitive to light in the red and far-red region of the visible spectrum. Many flowering plants use it to regulate the time of flowering based on the length of day and night (photoperiodism) and to set circadian rhythms. It also regulates other responses including the germination of seeds (photoblasty), elongation of seedlings, the size, shape and number of leaves, the synthesis of chlorophyll, and the straightening of the epicotyl or hypocotyl hook of dicot seedlings. It is found in the leaves of most plants.

Bacterial Flagellar Base
A flagellum is a lash-like appendage that protrudes from the cell body of certain prokaryotic and eukaryotic cells. The word flagellum in Latin means whip. The primary role of the flagellum is locomotion, but it also often has function as a sensory organelle, being sensitive to chemicals and temperatures outside the cell. Flagella are organelles defined by function rather than structure. Large differences occur between different types of flagella; the prokaryotic and eukaryotic flagella differ greatly in protein composition, structure, and mechanism of propulsion. However, both can be used for swimming.

ATP Synthase
ATP Synthase (also known as F-Type ATPase ), is an ATPase found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It uses a proton gradient to drive ATP synthesis by allowing the passive flux of protons across the membrane down their electrochemical gradient and using the energy released by the transport reaction to release newly formed ATP from the active site of F-ATPase. In some bacteria, sodium ions may be used instead.

As a member of the Bacteriology Department at the University of Wisconsin-Madison, Dr. Forest’s research focus is on the structures of bacterial proteins.

Ph: 1-608-265-3566
Email: Katrina T. Forest

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