Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)

Ice-associated algae produce ice-binding proteins (IBPs) to prevent freezing damage. The IBPs of the three chlorophytes that have been examined so far share little similarity across species, making it likely that they were acquired by horizontal gene transfer (HGT). To clarify the importance and sou...

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Published in:Journal of Phycology
Main Authors: Raymond, James A., Morgan-Kiss, Rachael
Format: Text
Language:English
Published: 2017
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5546997/
http://www.ncbi.nlm.nih.gov/pubmed/28543018
https://doi.org/10.1111/jpy.12550
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spelling ftpubmed:oai:pubmedcentral.nih.gov:5546997 2023-05-15T14:07:12+02:00 Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae) Raymond, James A. Morgan-Kiss, Rachael 2017-07-05 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5546997/ http://www.ncbi.nlm.nih.gov/pubmed/28543018 https://doi.org/10.1111/jpy.12550 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5546997/ http://www.ncbi.nlm.nih.gov/pubmed/28543018 http://dx.doi.org/10.1111/jpy.12550 Article Text 2017 ftpubmed https://doi.org/10.1111/jpy.12550 2018-08-05T00:13:42Z Ice-associated algae produce ice-binding proteins (IBPs) to prevent freezing damage. The IBPs of the three chlorophytes that have been examined so far share little similarity across species, making it likely that they were acquired by horizontal gene transfer (HGT). To clarify the importance and source of IBPs in chlorophytes, we sequenced the IBP genes of another Antarctic chlorophyte, Chlamydomonas sp. ICE-MDV (Chlamy-ICE). Genomic DNA and total RNA were sequenced and screened for known ice-associated genes. Chlamy-ICE has as many as 50 IBP isoforms, indicating that they have an important role in survival. The IBPs are of the DUF3494 type and have similar exon structures. The DUF3494 sequences are much more closely related to prokaryotic sequences than they are to sequences in other chlorophytes, and the chlorophyte IBP and ribosomal 18S phylogenies are dissimilar. The multiple IBP isoforms found in Chlamy-ICE and other algae may allow the algae to adapt to a greater variety of ice conditions than prokaryotes, which typically have a single IBP gene. The predicted structure of the DUF3494 domain has an ice-binding face with an orderly array of hydrophilic side chains. The results indicate that Chlamy-ICE acquired its IBP genes by HGT in a single event. The acquisitions of IBP genes by this and other species of Antarctic algae by HGT appear to be key evolutionary events that allowed algae to extend their ranges into polar environments. Text Antarc* Antarctic PubMed Central (PMC) Antarctic Journal of Phycology 53 4 848 854
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Article
spellingShingle Article
Raymond, James A.
Morgan-Kiss, Rachael
Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)
topic_facet Article
description Ice-associated algae produce ice-binding proteins (IBPs) to prevent freezing damage. The IBPs of the three chlorophytes that have been examined so far share little similarity across species, making it likely that they were acquired by horizontal gene transfer (HGT). To clarify the importance and source of IBPs in chlorophytes, we sequenced the IBP genes of another Antarctic chlorophyte, Chlamydomonas sp. ICE-MDV (Chlamy-ICE). Genomic DNA and total RNA were sequenced and screened for known ice-associated genes. Chlamy-ICE has as many as 50 IBP isoforms, indicating that they have an important role in survival. The IBPs are of the DUF3494 type and have similar exon structures. The DUF3494 sequences are much more closely related to prokaryotic sequences than they are to sequences in other chlorophytes, and the chlorophyte IBP and ribosomal 18S phylogenies are dissimilar. The multiple IBP isoforms found in Chlamy-ICE and other algae may allow the algae to adapt to a greater variety of ice conditions than prokaryotes, which typically have a single IBP gene. The predicted structure of the DUF3494 domain has an ice-binding face with an orderly array of hydrophilic side chains. The results indicate that Chlamy-ICE acquired its IBP genes by HGT in a single event. The acquisitions of IBP genes by this and other species of Antarctic algae by HGT appear to be key evolutionary events that allowed algae to extend their ranges into polar environments.
format Text
author Raymond, James A.
Morgan-Kiss, Rachael
author_facet Raymond, James A.
Morgan-Kiss, Rachael
author_sort Raymond, James A.
title Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)
title_short Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)
title_full Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)
title_fullStr Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)
title_full_unstemmed Multiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)
title_sort multiple ice-binding proteins of probable prokaryotic origin in an antarctic lake alga, chlamydomonas sp. ice-mdv (chlorophyceae)
publishDate 2017
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5546997/
http://www.ncbi.nlm.nih.gov/pubmed/28543018
https://doi.org/10.1111/jpy.12550
geographic Antarctic
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genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5546997/
http://www.ncbi.nlm.nih.gov/pubmed/28543018
http://dx.doi.org/10.1111/jpy.12550
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container_title Journal of Phycology
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container_issue 4
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