Research in the Leney lab focuses on protein post-translational modifications and how they control protein function. The multiple projects that are being undertaken within the group are detailed below.
Understanding Algae's macromolecular machines
Red microalgae live deep in ocean/lakes where sunlight is lacking, thus their photosynthetic machinery (termed phycobilisomes) have evolved to operate very efficiently. We are interested in determining how the phycobilisome functions and what makes it so efficient. Moreover, any knowledge obtained can be used in the design of new synthetic complexes that have potential for use within the solar power industry.
Due to their environmental habitat, the proteins within phycobilisomes need to transmit light at different wavelengths. Thus, the protein complexes within phycobilisomes are differently coloured; red, blue and green. In addition, these colourful complexes posses fluorescent properties. The protein complexes within phycobilisomes alone, therefore, have interesting biotechnological applications. One example being phycocyanin, a natural blue food colourant in bubble gum and jelly. We are using a variety of mass spectrometry techniques to characterise more of these colourful and fluorescent protein complexes for subsequent use in various biotechnological applications.
Unravelling the complexes mechanisms behind protein communication
Proteins do not function all of the time. Moreover, they constantly switch between active and inactive states. The activity of proteins are controlled predominantly by post-translational modifications (PTMs), yet how these PTMs do this is only beginning to be understood. PTMs can affect proteins in different ways and hundreds of different types of PTMs exist that all can modify the proteins uniquely which alters their function. With over 10,000 proteins in humans all being affected, painting the overall picture of the role PTMs play in cells is challenging. Yet, we know that a single incorrect switch/change in PTM status of a single protein can result in diseases such as cancer, neurological disorders and diabetes.
Our research aims to unravel this complex phenomenon. We focus on using mass spectrometry to unravel PTM crosstalk; the phenomenon whereby the modification of one residue within a protein alters the modification of another. Indeed, mass spectrometry can uniquely separate most PTMs by a change in mass. Through identifying these scenarios we aim to role out when PTMs cannot occur and thus unravel the complexity behind the role of protein PTMs on protein function.
Development of mass spectrometry methodology to monitor protein post-translational modifications and their roles in cells
Post-translational modifications (PTMs) can decipher whether a protein binds to its binding partner or not. For example, phosphorylation of C-terminal domain of RNA polymerase can increase its binding affinity to the cis-trans isomerase Pin1 compared to its unmodified counterpart. Moreover, this switch-mediated binding can have advantages as well as disadvantages depending on its context. We are interested in understanding more about the PTM-mediated binding events that occur in cells. Specifically, our research focuses on method development that aims to determine binding interfaces between proteins containing PTMs and their binding partners.