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Ice‐binding proteins and the ‘domain of unknown function’ 3494 family
Author(s) -
Vance Tyler D. R.,
BayerGiraldi Maddalena,
Davies Peter L.,
Mangiagalli Marco
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14764
Subject(s) - antifreeze protein , biophysics , ice nucleus , bacteria , chemistry , biology , microbiology and biotechnology , crystallography , biochemistry , nucleation , genetics , organic chemistry
Ice‐binding proteins ( IBP s) 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 IBP s. DUF 3494 IBP s 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, DUF 3494 IBP s 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 IBP s, which promise to leave their mark on several research fields including structural biology, protein biochemistry and cryobiology.