Ice‐binding proteins and the 'domain of unknown function' 3494 family. (9th February 2019)

• Record Type: Journal Article
• Authors: Vance, Tyler D. R.; Bayer‐Giraldi, Maddalena; Davies, Peter L.; Mangiagalli, Marco
• Is Part Of: FEBS journal. Volume 286:Number 5(2019)
• Page Start: 855
• Page End: 873
• Publication Date: 2019-02-09
• Subjects: DUF 3494 -- IBP‐1 fold -- ice recrystallization inhibition -- ice‐binding protein -- thermal hysteresis; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pathology, Molecular -- Periodicals; 572
• DOI: 10.1111/febs.14764
• Languages: English
• ISSNs: 1742-464X

Abstract

Abstract : Ice‐binding proteins (IBPs) control the growth and shape of ice crystals to cope with subzero temperatures in psychrophilic and freeze‐tolerant organisms. Recently, numerous proteins containing the domain of unknown function (DUF) 3494 were found to bind ice crystals and, hence, are classified as IBPs. DUF3494 IBPs constitute today the most widespread of the known IBP families. They can be found in different organisms including bacteria, yeasts and microalgae, supporting the hypothesis of horizontal transfer of its gene. Although the 3D structure is always a discontinuous β‐solenoid with a triangular cross‐section and an adjacent alpha‐helix, DUF3494 IBPs present very diverse activities in terms of the magnitude of their thermal hysteresis and inhibition of ice recrystallization. The proteins are secreted into the environments around the host cells or are anchored on their cell membranes. This review covers several aspects of this new class of IBPs, which promise to leave their mark on several research fields including structural biology, protein biochemistry and cryobiology. Abstract : Many psychrophilic microorganisms have proteins that contain the domain of unknown function (DUF) 3494. All analysed examples of this domain share the same discontinuous β‐solenoid fold and the ability to bind ice crystals, marking DUF3494 as a signature for a new class of ice‐binding proteins reviewed here. Despite these similarities, the members of this class are diverse in their biological sources, abilities to control ice growth and potential biological functions.