Structure of a bacterial ice binding protein with two faces of interaction with ice

Mangiagalli, Marco; Sarusi, Guy; Kaleda, Aleksei; Dolev, Maya Bar; Nardone, Valentina; Vena, V.F.; Braslavsky, Ido; Lotti, Marina; Nardini, M.

doi:10.1111/febs.14434

Cited by 25 publications

(43 citation statements)

References 51 publications

(109 reference statements)

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“…Interestingly, according to present day knowledge, all moderate basal‐binder IBPs share a β‐solenoid structure , which is also common to hyperactive ones. This observation suggests that the affinity for the basal plane benefits from the regular spacing of amino acid residues provided by β‐solenoid structure .…”

Section: Activity Of Duf3494 Ibpsmentioning

confidence: 99%

“…A) being the most representative (~ 68%). Almost all characterized DUF3494 IBPs exhibit this simple architecture . Generally, single‐DUF3494 IBPs also contain an N‐terminal signal peptide, suggesting that these proteins are secreted into the environment near the cells or accumulate in the membrane .…”

Section: Architecture Of Duf3494 Ibpsmentioning

confidence: 99%

“…Currently, nine crystal structures have been reported for DUF3494 IBP family members: Tis IBP6 , Tis IBP8 , Leucosporidium sp. AY30 IBP ( Le IBP) , Ff IBP , Col IBP , IBPv , Sf IBP_1 , Efc IBP and fc IBP11 . All these proteins present the IBP‐1 fold that consists of a discontinuous right‐handed β‐solenoid with a triangular cross‐section formed by three parallel β‐sheets (faces a, b and c), and an α helix that runs along the a‐face, parallel to the main axis of the protein (Fig.…”

Section: Structural Features Of Ibps Belonging To Duf3494mentioning

confidence: 99%

“…Structural biology and rational mutagenesis studies with the DUF3494 IBS have stressed the relevance of the b face of the β‐solenoid in ice‐binding, as well as of the loops that connect the a and b face . An exception is Efc IBP, which can bind ice crystals through both b and c faces . MD simulations with fc IBP11 have suggested other loops, not flat surfaces, like the α helix and the loop between the b‐ and the c‐face, are involved in ice‐binding .…”

Section: Ice‐binding Sites (Ibs) Of Duf3494 Ibpsmentioning

confidence: 99%

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Ice‐binding proteins and the ‘domain of unknown function’ 3494 family

et al. 2019

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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.

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Section: Activity Of Duf3494 Ibpsmentioning

confidence: 99%

Section: Architecture Of Duf3494 Ibpsmentioning

confidence: 99%

Section: Structural Features Of Ibps Belonging To Duf3494mentioning

confidence: 99%

Section: Ice‐binding Sites (Ibs) Of Duf3494 Ibpsmentioning

confidence: 99%

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Ice‐binding proteins and the ‘domain of unknown function’ 3494 family

et al. 2019

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“…CSPs control the expression of cold‐induced genes, such as antiterminators (Bae, Xia, Inouye, & Severinov, 2000). LAB are known to produce cold‐adapted enzymes that maintain activity at freezing temperatures and support both transcription and translation (Mangiagalli et al., 2018). Some LAB are also equipped with antifreeze proteins that bind to ice crystals and prevent them from piercing the cells (Polo et al., 2017).…”

Section: Environmental Stressesmentioning

confidence: 99%

Updates on understanding of probiotic lactic acid bacteria responses to environmental stresses and highlights on proteomic analyses

Mbye

Baig

AbuQamar

et al. 2020

Comp Rev Food Sci Food Safe

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Probiotics are defined as live microorganisms that improve the health of the host when administered in adequate quantities. Nonetheless, probiotics encounter extreme environmental conditions during food processing or along the gastrointestinal tract. This review discusses different environmental stresses that affect probiotics during food preparation, storage, and along the alimentary canal, including high temperature, low temperature, low and alkaline pH, oxidative stress, high hydrostatic pressure, osmotic pressure, and starvation. The understanding of how probiotics deal with environmental stress and thrive provides useful information to guide the selection of the strains with enhanced performance in specific situations, in food processing or during gastrointestinal transit. In most cases, multiple biological functions are affected upon exposure of the cell to environmental stress. Sensing of sublethal environmental stress can allow for adaptation processes to occur, which can include alterations in the expression of specific proteins.

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