Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases

Neil J. Oldfield, Fariza Shams, Karl G. Wooldridge, and David P.J. Turner

Molecular Bacteriology and Immunology Group, School of Life Sciences, Centre for Biomolecular Sciences, University of Nottingham, Nottingham, UK

Introduction

Moonlighting proteins are multifunctional proteins which perform two or more biochemical functions using a single polypeptide chain (Jeffery 1999, 2014; see Chapter 1). Moonlighting proteins have been documented in diverse organisms, including archaea (Jia et al. 2013), bacteria (Henderson and Martin 2011), yeasts (Gancedo and Flores 2008), eukaryotic parasites (Ginger 2014), plants (Moore 2004), and vertebrates (Kim and Dang 2005). Pathogenic bacterial species, such as Mycobacterium tuberculosis, Streptococcus pyogenes, Streptococcus pneumoniae, and Staphylococcus aureus, often employ multiple moonlighting proteins to enhance their pathogenic potential (Henderson 2014). Common examples are cytosolic enzymes or chaperones which moonlight as adhesion receptors, plasminogen-binding proteins, or immunomodulators on the bacterial cell surface (Wang et al. 2013). In particular, several enzymes of the Embden-Meyerhof-Parnas (EMP) glycolytic pathway, including fructose 1,6-bisphosphate aldolase (FBA), glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and enolase, have been shown to exhibit moonlighting functions on the bacterial surface (Henderson and Martin 2011).

 
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