MelampsoraV2, PubMed, Corpus, bibRecord, 000055

Genome-wide survey and characterization of the small heat shock protein gene family in Bursaphelenchus xylophilus.

Identifieur interne : 000055 ( PubMed/Corpus ); précédent : 000054; suivant : 000056

Genome-wide survey and characterization of the small heat shock protein gene family in Bursaphelenchus xylophilus.

Auteurs : Feng Wang ; Danlei Li ; Qiaoli Chen ; Ling Ma

Source :

Gene [ 1879-0038 ] ; 2016.

RBID : pubmed:26723508

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Body Temperature Regulation (genetics), Body Temperature Regulation (physiology), Evolution, Molecular (MeSH), Genome (MeSH), Heat-Shock Proteins, Small (genetics), Multigene Family (genetics), Phylogeny (MeSH), Tylenchida (genetics).
MESH :
- chemical , genetics : Heat-Shock Proteins, Small.
- genetics : Body Temperature Regulation, Multigene Family, Tylenchida.
- physiology : Body Temperature Regulation.
- Amino Acid Sequence, Animals, Evolution, Molecular, Genome, Phylogeny.

Abstract

Temperatures directly influence the distribution and intensity of pine wilt disease, which is caused by the pine wood nematode Bursaphelenchus xylophilus. Small heat shock proteins (sHSPs) are molecular chaperones that contribute to nematode survival during the stress response to high temperatures. Seven B. xylophilus sHSPs (Bx-sHSPs) were identified and studied in a whole-genome shotgun project. The replacement of aromatic amino acids with aliphatic amino acids in motifs was the most significant difference between Bx-sHSPs and Caenorhabditis elegans sHSPs (Ce-sHSPs). In Bx-sHSPs, two motifs showed consensus sequences similar to the known palindromic nGAAn sequence or variants of this sequence. A phylogenetic tree of Bx-sHSPs and corresponding Ce-sHSPs suggests the existence of a one-to-one orthologous relationship for all sHSPs. Gene evolution patterns corresponding to both purifying selection and positive selection were found in orthologous pairs of Ce-sHSPs and Bx-sHSPs. The upregulation of Bx-sHSPs in response to heat stress (30°C) suggests that these proteins play a role in thermoregulation.

DOI: 10.1016/j.gene.2015.12.047
PubMed: 26723508

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pubmed:26723508

Le document en format XML

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<author><name sortKey="Wang, Feng" sort="Wang, Feng" uniqKey="Wang F" first="Feng" last="Wang">Feng Wang</name>
<affiliation><nlm:affiliation>College of Forestry, Northeast Forestry University, Harbin 150040, China. Electronic address: kingsummit@126.com.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Li, Danlei" sort="Li, Danlei" uniqKey="Li D" first="Danlei" last="Li">Danlei Li</name>
<affiliation><nlm:affiliation>College of Forestry, Northeast Forestry University, Harbin 150040, China. Electronic address: danleili@nefu.edu.cn.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Chen, Qiaoli" sort="Chen, Qiaoli" uniqKey="Chen Q" first="Qiaoli" last="Chen">Qiaoli Chen</name>
<affiliation><nlm:affiliation>College of Forestry, Northeast Forestry University, Harbin 150040, China. Electronic address: melampsora@126.com.</nlm:affiliation>
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<author><name sortKey="Ma, Ling" sort="Ma, Ling" uniqKey="Ma L" first="Ling" last="Ma">Ling Ma</name>
<affiliation><nlm:affiliation>College of Forestry, Northeast Forestry University, Harbin 150040, China. Electronic address: biocontrol@sina.com.</nlm:affiliation>
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<author><name sortKey="Li, Danlei" sort="Li, Danlei" uniqKey="Li D" first="Danlei" last="Li">Danlei Li</name>
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<author><name sortKey="Ma, Ling" sort="Ma, Ling" uniqKey="Ma L" first="Ling" last="Ma">Ling Ma</name>
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<term>Body Temperature Regulation (physiology)</term>
<term>Evolution, Molecular (MeSH)</term>
<term>Genome (MeSH)</term>
<term>Heat-Shock Proteins, Small (genetics)</term>
<term>Multigene Family (genetics)</term>
<term>Phylogeny (MeSH)</term>
<term>Tylenchida (genetics)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Heat-Shock Proteins, Small</term>
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<term>Multigene Family</term>
<term>Tylenchida</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Body Temperature Regulation</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
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<front><div type="abstract" xml:lang="en">Temperatures directly influence the distribution and intensity of pine wilt disease, which is caused by the pine wood nematode Bursaphelenchus xylophilus. Small heat shock proteins (sHSPs) are molecular chaperones that contribute to nematode survival during the stress response to high temperatures. Seven B. xylophilus sHSPs (Bx-sHSPs) were identified and studied in a whole-genome shotgun project. The replacement of aromatic amino acids with aliphatic amino acids in motifs was the most significant difference between Bx-sHSPs and Caenorhabditis elegans sHSPs (Ce-sHSPs). In Bx-sHSPs, two motifs showed consensus sequences similar to the known palindromic nGAAn sequence or variants of this sequence. A phylogenetic tree of Bx-sHSPs and corresponding Ce-sHSPs suggests the existence of a one-to-one orthologous relationship for all sHSPs. Gene evolution patterns corresponding to both purifying selection and positive selection were found in orthologous pairs of Ce-sHSPs and Bx-sHSPs. The upregulation of Bx-sHSPs in response to heat stress (30°C) suggests that these proteins play a role in thermoregulation. </div>
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<Title>Gene</Title>
<ISOAbbreviation>Gene</ISOAbbreviation>
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<ArticleTitle>Genome-wide survey and characterization of the small heat shock protein gene family in Bursaphelenchus xylophilus.</ArticleTitle>
<Pagination><MedlinePgn>153-61</MedlinePgn>
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<Abstract><AbstractText>Temperatures directly influence the distribution and intensity of pine wilt disease, which is caused by the pine wood nematode Bursaphelenchus xylophilus. Small heat shock proteins (sHSPs) are molecular chaperones that contribute to nematode survival during the stress response to high temperatures. Seven B. xylophilus sHSPs (Bx-sHSPs) were identified and studied in a whole-genome shotgun project. The replacement of aromatic amino acids with aliphatic amino acids in motifs was the most significant difference between Bx-sHSPs and Caenorhabditis elegans sHSPs (Ce-sHSPs). In Bx-sHSPs, two motifs showed consensus sequences similar to the known palindromic nGAAn sequence or variants of this sequence. A phylogenetic tree of Bx-sHSPs and corresponding Ce-sHSPs suggests the existence of a one-to-one orthologous relationship for all sHSPs. Gene evolution patterns corresponding to both purifying selection and positive selection were found in orthologous pairs of Ce-sHSPs and Bx-sHSPs. The upregulation of Bx-sHSPs in response to heat stress (30°C) suggests that these proteins play a role in thermoregulation. </AbstractText>
<CopyrightInformation>Copyright © 2015. Published by Elsevier B.V.</CopyrightInformation>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Bursaphelenchus xylophilus</Keyword>
<Keyword MajorTopicYN="N">Genome</Keyword>
<Keyword MajorTopicYN="N">Heat shock</Keyword>
<Keyword MajorTopicYN="N">Pine wilt</Keyword>
<Keyword MajorTopicYN="N">sHSP</Keyword>
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Genome-wide survey and characterization of the small heat shock protein gene family in Bursaphelenchus xylophilus.

Genome-wide survey and characterization of the small heat shock protein gene family in Bursaphelenchus xylophilus.

Source :

English descriptors

Abstract

Links to Exploration step

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