Cargando…

Bacterial Ice Crystal Controlling Proteins

Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large...

Descripción completa

Detalles Bibliográficos
Autores principales: Lorv, Janet S. H., Rose, David R., Glick, Bernard R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3918373/
https://www.ncbi.nlm.nih.gov/pubmed/24579057
http://dx.doi.org/10.1155/2014/976895
_version_ 1782302956863881216
author Lorv, Janet S. H.
Rose, David R.
Glick, Bernard R.
author_facet Lorv, Janet S. H.
Rose, David R.
Glick, Bernard R.
author_sort Lorv, Janet S. H.
collection PubMed
description Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large ice crystals, while ice nucleation proteins induce formation of embryonic ice crystals. Although both protein classes have differing functions, these proteins use the same ice binding mechanisms. Rather than direct binding, it is probable that these protein classes create an ice surface prior to ice crystal surface adsorption. Function is differentiated by molecular size of the protein. This paper reviews the similar and different aspects of bacterial antifreeze and ice nucleation proteins, the role of these proteins in freezing tolerance, prevalence of these proteins in psychrophiles, and current mechanisms of protein-ice interactions.
format Online
Article
Text
id pubmed-3918373
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-39183732014-02-26 Bacterial Ice Crystal Controlling Proteins Lorv, Janet S. H. Rose, David R. Glick, Bernard R. Scientifica (Cairo) Review Article Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large ice crystals, while ice nucleation proteins induce formation of embryonic ice crystals. Although both protein classes have differing functions, these proteins use the same ice binding mechanisms. Rather than direct binding, it is probable that these protein classes create an ice surface prior to ice crystal surface adsorption. Function is differentiated by molecular size of the protein. This paper reviews the similar and different aspects of bacterial antifreeze and ice nucleation proteins, the role of these proteins in freezing tolerance, prevalence of these proteins in psychrophiles, and current mechanisms of protein-ice interactions. Hindawi Publishing Corporation 2014 2014-01-20 /pmc/articles/PMC3918373/ /pubmed/24579057 http://dx.doi.org/10.1155/2014/976895 Text en Copyright © 2014 Janet S. H. Lorv et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Lorv, Janet S. H.
Rose, David R.
Glick, Bernard R.
Bacterial Ice Crystal Controlling Proteins
title Bacterial Ice Crystal Controlling Proteins
title_full Bacterial Ice Crystal Controlling Proteins
title_fullStr Bacterial Ice Crystal Controlling Proteins
title_full_unstemmed Bacterial Ice Crystal Controlling Proteins
title_short Bacterial Ice Crystal Controlling Proteins
title_sort bacterial ice crystal controlling proteins
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3918373/
https://www.ncbi.nlm.nih.gov/pubmed/24579057
http://dx.doi.org/10.1155/2014/976895
work_keys_str_mv AT lorvjanetsh bacterialicecrystalcontrollingproteins
AT rosedavidr bacterialicecrystalcontrollingproteins
AT glickbernardr bacterialicecrystalcontrollingproteins