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Oligomerization of the P. aeruginosa Aer-z N-terminal Domain May Determine Signaling State

CSEF · 2009 Biochemistry/ Molecular Biology

Danielle P. Monahan · Colton High School, Colton, San Bernardino County

Overview

Objectives/Goals The goal was to determine if the N-terminal domain of the Aer-z affects oligomerization of the receptor when it is oxidized or reduced. Methods/Materials P. aeroginosa fragments Aer-z PAS 173-289 was examined as a compact monomer in oxidized and reduced states. Results Aer-z PAS 173-289 elevated as compact monomer in oxidized and reduced states. N-terminal domain Aer-z-289 elevated as a compact monomer when oxidized but not when reduced. Conclusions/Discussion Aer-z N-terminal domain assumes different conformations in different signaling states and suggests that oligomerization is associated and interacts with a loss of signaling.

Summary statement

The goal was to determine if the N-terminal domain of the Aer-z affects oligomerization of the receptor when its oxidized or reduced.

Help received

Used lab equipment at Loma Linda University under the supervision of Dr. Watts and Dr. Taylor in a summer immersion program.

Competition history

  • CSEF 2009 Biochemistry/ Molecular Biology · Entry S0421

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