Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean

Ice-binding proteins (IBPs) are a group of ecologically and biotechnologically relevant enzymes produced by psychrophilic organisms. Although putative IBPs containing the domain of unknown function (DUF) 3494 have been identified in many taxa of polar microbes, our knowledge of their genetic and str...
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Autor*in:	Johanna C. Winder [verfasserIn] William Boulton [verfasserIn] Asaf Salamov [verfasserIn] Sarah Lena Eggers [verfasserIn] Katja Metfies [verfasserIn] Vincent Moulton [verfasserIn] Thomas Mock [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	metagenomics MAGs ice-binding proteins DUF3494 domain shuffling polar genomics

Übergeordnetes Werk:	In: Genes - MDPI AG, 2010, 14(2023), 2, p 363
Übergeordnetes Werk:	volume:14 ; year:2023 ; number:2, p 363

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/genes14020363

Katalog-ID:	DOAJ080283411

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520			\|a Ice-binding proteins (IBPs) are a group of ecologically and biotechnologically relevant enzymes produced by psychrophilic organisms. Although putative IBPs containing the domain of unknown function (DUF) 3494 have been identified in many taxa of polar microbes, our knowledge of their genetic and structural diversity in natural microbial communities is limited. Here, we used samples from sea ice and sea water collected in the central Arctic Ocean as part of the MOSAiC expedition for metagenome sequencing and the subsequent analyses of metagenome-assembled genomes (MAGs). By linking structurally diverse IBPs to particular environments and potential functions, we reveal that IBP sequences are enriched in interior ice, have diverse genomic contexts and cluster taxonomically. Their diverse protein structures may be a consequence of domain shuffling, leading to variable combinations of protein domains in IBPs and probably reflecting the functional versatility required to thrive in the extreme and variable environment of the central Arctic Ocean.
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language	English
source	In Genes 14(2023), 2, p 363 volume:14 year:2023 number:2, p 363
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authorswithroles_txt_mv	Johanna C. Winder @@aut@@ William Boulton @@aut@@ Asaf Salamov @@aut@@ Sarah Lena Eggers @@aut@@ Katja Metfies @@aut@@ Vincent Moulton @@aut@@ Thomas Mock @@aut@@
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author	Johanna C. Winder
spellingShingle	Johanna C. Winder misc QH426-470 misc metagenomics misc MAGs misc ice-binding proteins misc DUF3494 misc domain shuffling misc polar genomics misc Genetics Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean
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topic_title	QH426-470 Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean metagenomics MAGs ice-binding proteins DUF3494 domain shuffling polar genomics
topic	misc QH426-470 misc metagenomics misc MAGs misc ice-binding proteins misc DUF3494 misc domain shuffling misc polar genomics misc Genetics
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title	Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean
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title_auth	Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean
abstract	Ice-binding proteins (IBPs) are a group of ecologically and biotechnologically relevant enzymes produced by psychrophilic organisms. Although putative IBPs containing the domain of unknown function (DUF) 3494 have been identified in many taxa of polar microbes, our knowledge of their genetic and structural diversity in natural microbial communities is limited. Here, we used samples from sea ice and sea water collected in the central Arctic Ocean as part of the MOSAiC expedition for metagenome sequencing and the subsequent analyses of metagenome-assembled genomes (MAGs). By linking structurally diverse IBPs to particular environments and potential functions, we reveal that IBP sequences are enriched in interior ice, have diverse genomic contexts and cluster taxonomically. Their diverse protein structures may be a consequence of domain shuffling, leading to variable combinations of protein domains in IBPs and probably reflecting the functional versatility required to thrive in the extreme and variable environment of the central Arctic Ocean.
abstractGer	Ice-binding proteins (IBPs) are a group of ecologically and biotechnologically relevant enzymes produced by psychrophilic organisms. Although putative IBPs containing the domain of unknown function (DUF) 3494 have been identified in many taxa of polar microbes, our knowledge of their genetic and structural diversity in natural microbial communities is limited. Here, we used samples from sea ice and sea water collected in the central Arctic Ocean as part of the MOSAiC expedition for metagenome sequencing and the subsequent analyses of metagenome-assembled genomes (MAGs). By linking structurally diverse IBPs to particular environments and potential functions, we reveal that IBP sequences are enriched in interior ice, have diverse genomic contexts and cluster taxonomically. Their diverse protein structures may be a consequence of domain shuffling, leading to variable combinations of protein domains in IBPs and probably reflecting the functional versatility required to thrive in the extreme and variable environment of the central Arctic Ocean.
abstract_unstemmed	Ice-binding proteins (IBPs) are a group of ecologically and biotechnologically relevant enzymes produced by psychrophilic organisms. Although putative IBPs containing the domain of unknown function (DUF) 3494 have been identified in many taxa of polar microbes, our knowledge of their genetic and structural diversity in natural microbial communities is limited. Here, we used samples from sea ice and sea water collected in the central Arctic Ocean as part of the MOSAiC expedition for metagenome sequencing and the subsequent analyses of metagenome-assembled genomes (MAGs). By linking structurally diverse IBPs to particular environments and potential functions, we reveal that IBP sequences are enriched in interior ice, have diverse genomic contexts and cluster taxonomically. Their diverse protein structures may be a consequence of domain shuffling, leading to variable combinations of protein domains in IBPs and probably reflecting the functional versatility required to thrive in the extreme and variable environment of the central Arctic Ocean.
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title_short	Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean
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Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean

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