Moonlighting proteins comprise a class of multifunctional proteins in which a single polypeptide chain has multiple biochemical functions that are not due to gene fusion events. For example, some cytosolic enzymes moonlight as transcription factors, crystallins, chaperones, extracellular growth factors, or cell surface adhesins. The variety of known moonlighting proteins, the multiple ways in which one protein can have multiple functions, the potential benefits to the organism of combining two functions in one protein, and the methods proposed for a protein to evolve a second function suggest that moonlighting proteins might be common.
The ability of a protein to moonlight in different multi-protein complexes or pathways can complicate the prediction of protein function from sequence or structure and the annotation of sequence databases. To date, most moonlighting functions have been found by serendipity. There is currently no straightforward method to identify which proteins moonlight, or for determining if a protein of interest is a moonlighting protein. In addition, sequence homologues of moonlighting proteins often do not perform both functions.
This research topic will include publications on many aspects of moonlighting proteins - examples of proteins that moonlight, structures of moonlighting proteins, their roles in diseases, how they may have evolved, moonlighting proteins and proteomics, bioinformatics of moonlighting proteins, etc.
Moonlighting proteins comprise a class of multifunctional proteins in which a single polypeptide chain has multiple biochemical functions that are not due to gene fusion events. For example, some cytosolic enzymes moonlight as transcription factors, crystallins, chaperones, extracellular growth factors, or cell surface adhesins. The variety of known moonlighting proteins, the multiple ways in which one protein can have multiple functions, the potential benefits to the organism of combining two functions in one protein, and the methods proposed for a protein to evolve a second function suggest that moonlighting proteins might be common.
The ability of a protein to moonlight in different multi-protein complexes or pathways can complicate the prediction of protein function from sequence or structure and the annotation of sequence databases. To date, most moonlighting functions have been found by serendipity. There is currently no straightforward method to identify which proteins moonlight, or for determining if a protein of interest is a moonlighting protein. In addition, sequence homologues of moonlighting proteins often do not perform both functions.
This research topic will include publications on many aspects of moonlighting proteins - examples of proteins that moonlight, structures of moonlighting proteins, their roles in diseases, how they may have evolved, moonlighting proteins and proteomics, bioinformatics of moonlighting proteins, etc.
