Cold adapted proteins
The aim of this work is to contribute to shed light on how cold-adapted proteins developed a molecular strategy to enhance their flexibility while still preserving sufficient stability to be functional. So far we solved the structure of a truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 (PDB-code: 4UUR; Giordano et al., 2015), a cytoglobin from the Antarctic fish Dissostichus mawsoni (PDB-code: 6Q6P; Giordano et al., 2020), a bacterial acyl aminoacyl peptidase from Sporosarcina psychrophila(PDB-code: 5L8S; Brocca et al., 2016), a beta galactosidase (PDB-code: 6Y2K; Mangiagalli et al., 2020) and a glycoside hydrolase GH1 (PDB-code: 8PUO; Gourlay et al., 2024) from the psychrophilic Marinomonas ef1. Our data shed further light on how these cold-adapted proteins developed a molecular strategy to enhance their flexibility while still preserving sufficient stability to be functional. Within this project line, we also solved the structure (at the atomic resolution of 0.84 Å) of an antifreeze protein from the Antarctic ciliate Euplotes focardii and the associated bacterial consortium (PDB-code: 6EIO). These kind of proteins are able to protect from freezing damage the organisms exposed to permanent sub-zero temperatures or seasonal temperature dropping and because of these properties it has been envisaged their potential in food processing, cryopreservation, cryosurgery, fishery and agricultural industries, and anti-ice materials development. Furthermore, this protein has been used as a target for the international project of Critical Assessment of protein Structure Prediction (CASP12) (http://predictioncenter.org/) to test sequence-based 3D structural predictions of proteins (Kryshtafovych et al., 2017).
Publications
Gourlay LJ, Mangiagalli M, Moroni E, Lotti M, Nardini M. Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1. FEBS J. 2024 Jul;291(13):2897-2917. doi: 10.1111/febs.17096 [PubMed: 38400529]
Erratum in: FEBS J. 2025 Jun;292(12):3264. doi: 10.1111/febs.70123. [Pubmed: 40318181]
Mangiagalli M, Lapi M, Maione S, Orlando M, Brocca S, Pesce A, Barbiroli A, Camilloni C, Pucciarelli S, Lotti M, Nardini M. The co-existence of cold activity and thermal stability in an Antarctic GH42 beta-galactosidase relies on its hexameric quaternary arrangement. FEBS J. 2020 May 4. doi: 10.1111/febs.15354. Epub ahead of print. [PubMec: 32363751].
Giordano D, Pesce A, Vermeylen S, Abbruzzetti S, Nardini M, Marchesani F, Berghmans H, Seira C, Bruno S, Javier Luque F, di Prisco G, Ascenzi P, Dewilde S, Bolognesi M, Viappiani C, Verde C. Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions. Comput Struct Biotechnol J. 2020 Aug 12;18:2132-2144. doi: 10.1016/j.csbj.2020.08.007. [PMID: 32913582]
Kryshtafovych A, Albrecht R, Basle A, Bule P, Caputo AT, Carvalho AL, Chao KL, Diskin R, Fidelis K, Fontes CMGA, Fredslund F, Gilbert HJ, Goulding CW, Hartmann MD, Hayes CS, Herzberg O, Hill JC, Joachimiak A, Kohring GW, Koning RI, Lo Leggio L, Mangiagalli M, Michalska K, Moult J, Najmudin S, Nardini M, Nardone V, Ndeh D, Nguyen TH, Pintacuda G, Postel S, van Raaij MJ, Roversi P, Shimon A, Singh AK, Sundberg EJ, Tars K, Zitzmann N, Schwede T. Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016). Proteins. 2017 Sep 28. doi: 10.1002/prot.25392. [Epub ahead of print] [PubMed: 28960539] Brocca S, Ferrari C, Barbiroli A, Pesce A, Lotti M, Nardini M. A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation. FEBS J. 2016 Dec;283(23):4310-4324. doi: 10.1111/febs.13925. [PubMed: 27739253]
Giordano D, Pesce A, Boechi L, Bustamante JP, Caldelli E, Howes BD, Riccio A, di Prisco G, Nardini M, Estrin D, Smulevich G, Bolognesi M, Verde C. Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. FEBS J. 2015 Aug;282(15):2948-65. doi: 10.1111/febs.13335. [PubMed: 26040838]
Cold adaptation Team
Louise Gourlay, Marco Nardini
Main collaborators
Prof. A. Pesce, University of Genova (Italy); Dr. D. Giordano, CNR-IBBR Naples (Italy); Prof. M. Lotti and Dr. M. Mangiagalli, University of Milano-Bicocca (Italy)