Heat Shock Proteins as Indicators of Stress in Marine Organisms
Supervisors Adele Pile, Murray Thomson.
Many newly expressed cellular proteins need a little help to fold
into their correct 3 dimensional structure and they are given this
help by specialized proteins that are referred to as molecular chaperones.
Heat shock proteins are a major family of molecular chaperones and
these proteins were discovered for their ability to help reform
the high levels of misfolded proteins that are produced by elevated
temperatures.
Other forms of stress such as pollution can cause cells to produce
proteins that are not properly folded into their normal structure
and these stressors can also elicit a heat shock protein response.
This response may be a powerful indicator of environmental stressors
in marine organisms but very little research has been done in this
area. This presents an exciting opportunity to work in the field
and the lab in studying the cellular effects of different types
of environmental stress on a range of marine creatures.
The Role of the HOXA10 Gene in Lizard Viviparity
Supervisors - Mike Thompson, Murray Thomson
Viviparity has evolved in lizards and snakes (squamates) over 100
times and these animals therefore provide an excellent model to
study the evolution of viviparity. Understanding the changes that
take place in the pre implantation uterus and the development of
the placenta are crucial in understanding the evolution of viviparity.
The goal of this project is to identify and quantify the expression
and activity of the developmental gene, HoxA10, in the uterus of
a viviparous lizard. This project combines techniques in histology
and proteomics to understand the role of HOXA10 in developmental
changes that prepare the lizard uterus for implantation.
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