Literature DB >> 16233340

The structures and functions of ice crystal-controlling proteins from bacteria.

Hidehisa Kawahara1.   

Abstract

Many organisms have evolved into unique mechanisms which minimize freezing injury due to extracellular ice formation. Specifically, certain bacteria have produced a few proteins each with different functions. For example, the ice nucleation protein acts as a template for ice formation, which is responsible for imparting ice nucleating activity. The anti-nucleating protein inhibits the fluctuation of ice nucleus formation by a foreign particle in the water drop. Also, the antifreeze proteins depress the freezing temperature, modify or suppress ice crystal growth, inhibit ice recrystallization, and protect the cell membrane from cold-induced damage. In this article, a review on the current knowledge of the structure and the function of these three types of proteins, which are capable of interacting with ice itself or its nuclei from bacteria.

Entities:  

Year:  2002        PMID: 16233340     DOI: 10.1016/s1389-1723(02)80185-2

Source DB:  PubMed          Journal:  J Biosci Bioeng        ISSN: 1347-4421            Impact factor:   2.894


  19 in total

1.  Surface display of domain III of Japanese encephalitis virus E protein on Salmonella typhimurium by using an ice nucleation protein.

Authors:  Jian-Lin Dou; Tao Jing; Jing-Jing Fan; Zhi-Ming Yuan
Journal:  Virol Sin       Date:  2011-12-10       Impact factor: 4.327

2.  Elementary steps at the surface of ice crystals visualized by advanced optical microscopy.

Authors:  Gen Sazaki; Salvador Zepeda; Shunichi Nakatsubo; Etsuro Yokoyama; Yoshinori Furukawa
Journal:  Proc Natl Acad Sci U S A       Date:  2010-10-25       Impact factor: 11.205

Review 3.  Some like it cold: understanding the survival strategies of psychrophiles.

Authors:  Pieter De Maayer; Dominique Anderson; Craig Cary; Don A Cowan
Journal:  EMBO Rep       Date:  2014-03-26       Impact factor: 8.807

4.  Ultrastructural analysis of the extracellular matter secreted by the psychrotolerant bacterium Pseudoalteromonas antarctica NF3.

Authors:  Maria Nevot; Victor Deroncele; Carmen López-Iglesias; Nuria Bozal; Jesús Guinea; Elena Mercade
Journal:  Microb Ecol       Date:  2006-04-28       Impact factor: 4.552

5.  Bacterial lipoteichoic acid enhances cryosurvival.

Authors:  Charles V Rice; Amy Middaugh; Jason R Wickham; Anthony Friedline; Kieth J Thomas; Erin Scull; Karen Johnson; Malcolm Zachariah; Ravindranth Garimella
Journal:  Extremophiles       Date:  2014-12-05       Impact factor: 2.395

6.  Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor.

Authors:  Xiaohu Shao; Mengtian Jiang; Ziniu Yu; Hao Cai; Lin Li
Journal:  Microb Cell Fact       Date:  2009-09-16       Impact factor: 5.328

Review 7.  Polysaccharide hydrolysis with engineered Escherichia coli for the production of biocommodities.

Authors:  Iván Muñoz-Gutiérrez; Alfredo Martinez
Journal:  J Ind Microbiol Biotechnol       Date:  2013-03-12       Impact factor: 3.346

8.  Molecular characterization of an ice nucleation protein variant (inaQ) from Pseudomonas syringae and the analysis of its transmembrane transport activity in Escherichia coli.

Authors:  Qianqian Li; Qi Yan; Jinsi Chen; Yan He; Jing Wang; Hongxing Zhang; Ziniu Yu; Lin Li
Journal:  Int J Biol Sci       Date:  2012-09-01       Impact factor: 6.580

9.  Experimental Warming Reduces Survival, Cold Tolerance, and Gut Prokaryotic Diversity of the Eastern Subterranean Termite, Reticulitermes flavipes (Kollar).

Authors:  Rachel A Arango; Sean D Schoville; Cameron R Currie; Camila Carlos-Shanley
Journal:  Front Microbiol       Date:  2021-05-17       Impact factor: 5.640

10.  Probing the Biomimetic Ice Nucleation Inhibition Activity of Poly(vinyl alcohol) and Comparison to Synthetic and Biological Polymers.

Authors:  Thomas Congdon; Bethany T Dean; James Kasperczak-Wright; Caroline I Biggs; Rebecca Notman; Matthew I Gibson
Journal:  Biomacromolecules       Date:  2015-08-14       Impact factor: 6.988

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