LeHavreV1, PubMed, Curation, bibRecord, 000121

An intron-containing, heat-inducible stress-70 gene in the millipede Tachypodoiulus niger (Julidae, Diplopoda).

Identifieur interne : 000121 ( PubMed/Curation ); précédent : 000120; suivant : 000122

An intron-containing, heat-inducible stress-70 gene in the millipede Tachypodoiulus niger (Julidae, Diplopoda).

Auteurs : Thomas Knigge [France] ; Lutz Bachmann ; Heinz-R Köhler

Source :

Cell stress & chaperones [ 1466-1268 ] ; 2014.

RBID : pubmed:24446070

Descripteurs français

Wicri :
- geographic : Niger.

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Arthropods (genetics), Arthropods (metabolism), Base Sequence, HSC70 Heat-Shock Proteins (genetics), HSC70 Heat-Shock Proteins (metabolism), Heat-Shock Proteins (metabolism), Heat-Shock Response (genetics), Hot Temperature, Introns, Niger.
MESH :
- chemical , genetics : HSC70 Heat-Shock Proteins.
- geographic : Niger.
- genetics : Arthropods, Heat-Shock Response.
- metabolism : Arthropods, HSC70 Heat-Shock Proteins, Heat-Shock Proteins.
- Amino Acid Sequence, Animals, Base Sequence, Hot Temperature, Introns.

Abstract

The highly conserved part of the nucleotide-binding domain of the hsp70 gene family was amplified from the soil diplopod Tachypodoiulus niger (Julidae, Diplopoda). Genomic DNA yielded 701, 549 and 540 bp sequences, whereas cDNA from heat shocked animals produced only one distinct fragment of 543 bp. The sequences could be classified as a 70 kDa heat shock protein (hsp70), the corresponding 70 kDa heat shock cognate (hsc70) and a glucose-related hsp70 homologue (grp78). Comparisons of genomic and cDNA sequences of hsc70 identified two introns within the consensus sequence. Generally, stress-70 expression levels were low, which hampered successful RT-PCR and subsequent subcloning. Following experimental heat shock, however, the spliced hsc70 was amplified predominantly, instead of its inducible homologue hsp70. This finding suggests that microevolution in this soil-dwelling arthropod is directed towards low constitutive stress-70 levels and that the capacity for stress-70 induction presumably is limited. hsc70, albeit having introns, apparently is inducible and contributes to the stress-70 response.

DOI: 10.1007/s12192-014-0494-7
PubMed: 24446070

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Le document en format XML

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<author><name sortKey="Knigge, Thomas" sort="Knigge, Thomas" uniqKey="Knigge T" first="Thomas" last="Knigge">Thomas Knigge</name>
<affiliation wicri:level="1"><nlm:affiliation>Laboratory of Ecotoxicology, EA 3222 PRES Normandie, Le Havre University, 25 Rue Philippe Lebon, F-76058, Le Havre Cedex, France, Thomas.Knigge@univ-lehavre.fr.</nlm:affiliation>
<country wicri:rule="url">France</country>
<wicri:regionArea>Laboratory of Ecotoxicology, EA 3222 PRES Normandie, Le Havre University, 25 Rue Philippe Lebon, F-76058, Le Havre Cedex, France</wicri:regionArea>
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<author><name sortKey="Bachmann, Lutz" sort="Bachmann, Lutz" uniqKey="Bachmann L" first="Lutz" last="Bachmann">Lutz Bachmann</name>
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<term>Arthropods (genetics)</term>
<term>Arthropods (metabolism)</term>
<term>Base Sequence</term>
<term>HSC70 Heat-Shock Proteins (genetics)</term>
<term>HSC70 Heat-Shock Proteins (metabolism)</term>
<term>Heat-Shock Proteins (metabolism)</term>
<term>Heat-Shock Response (genetics)</term>
<term>Hot Temperature</term>
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<term>Niger</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arthropods</term>
<term>Heat-Shock Response</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arthropods</term>
<term>HSC70 Heat-Shock Proteins</term>
<term>Heat-Shock Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Base Sequence</term>
<term>Hot Temperature</term>
<term>Introns</term>
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<keywords scheme="Wicri" type="geographic" xml:lang="fr"><term>Niger</term>
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<front><div type="abstract" xml:lang="en">The highly conserved part of the nucleotide-binding domain of the hsp70 gene family was amplified from the soil diplopod Tachypodoiulus niger (Julidae, Diplopoda). Genomic DNA yielded 701, 549 and 540 bp sequences, whereas cDNA from heat shocked animals produced only one distinct fragment of 543 bp. The sequences could be classified as a 70 kDa heat shock protein (hsp70), the corresponding 70 kDa heat shock cognate (hsc70) and a glucose-related hsp70 homologue (grp78). Comparisons of genomic and cDNA sequences of hsc70 identified two introns within the consensus sequence. Generally, stress-70 expression levels were low, which hampered successful RT-PCR and subsequent subcloning. Following experimental heat shock, however, the spliced hsc70 was amplified predominantly, instead of its inducible homologue hsp70. This finding suggests that microevolution in this soil-dwelling arthropod is directed towards low constitutive stress-70 levels and that the capacity for stress-70 induction presumably is limited. hsc70, albeit having introns, apparently is inducible and contributes to the stress-70 response.</div>
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<Abstract><AbstractText>The highly conserved part of the nucleotide-binding domain of the hsp70 gene family was amplified from the soil diplopod Tachypodoiulus niger (Julidae, Diplopoda). Genomic DNA yielded 701, 549 and 540 bp sequences, whereas cDNA from heat shocked animals produced only one distinct fragment of 543 bp. The sequences could be classified as a 70 kDa heat shock protein (hsp70), the corresponding 70 kDa heat shock cognate (hsc70) and a glucose-related hsp70 homologue (grp78). Comparisons of genomic and cDNA sequences of hsc70 identified two introns within the consensus sequence. Generally, stress-70 expression levels were low, which hampered successful RT-PCR and subsequent subcloning. Following experimental heat shock, however, the spliced hsc70 was amplified predominantly, instead of its inducible homologue hsp70. This finding suggests that microevolution in this soil-dwelling arthropod is directed towards low constitutive stress-70 levels and that the capacity for stress-70 induction presumably is limited. hsc70, albeit having introns, apparently is inducible and contributes to the stress-70 response.</AbstractText>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<MeshHeading><DescriptorName UI="D050883" MajorTopicYN="N">HSC70 Heat-Shock Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D006360" MajorTopicYN="N">Heat-Shock Proteins</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D018869" MajorTopicYN="N">Heat-Shock Response</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007438" MajorTopicYN="N">Introns</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009548" MajorTopicYN="N" Type="Geographic">Niger</DescriptorName>
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An intron-containing, heat-inducible stress-70 gene in the millipede Tachypodoiulus niger (Julidae, Diplopoda).

An intron-containing, heat-inducible stress-70 gene in the millipede Tachypodoiulus niger (Julidae, Diplopoda).

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Abstract

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