Identification and characterization of the putative oscillator protein, VDAC, in Aplysia californica.

摘要

The rhythmic, daily timing of changes in an organism's physiology and behavior is controlled by an endogenous circadian oscillator. Based on the adaptation to Earth's daily rotation about its axis, this wonderfully precise timing mechanism exists in nearly every species of organism examined--in multicellular and single cell plants and animals--even bacteria.;Analysis of circadian rhythms has evolved from physiological and behavioral studies to the examination of the molecular composition of the timing mechanism. Based on studies in numerous organisms, a molecular model for the clock has developed which is based on the transcription and translation of key proteins. Using genetic and molecular techniques, a few genes coding for bona fide clock proteins have been identified in Drosophila and Neurospora. Using a molecular approach, a number of putative clock proteins have been identified in the marine mollusk Aplysia californica. The general objective of this research was to analyze the role of one of these putative oscillator proteins, specifically the voltage-dependent anion channel protein (VDAC), by examining the effects of phase shifting treatments on both the protein and the mRNA level. In addition, immunoreactive techniques were used to identify the cellular location of VDAC in the Aplysia eye and to demonstrate the presence of VDAC in the plasma membrane of Aplysia neurons.