An intron-containing, heat-inducible stress-70 gene in the millipede Tachypodoiulus niger (Julidae, Diplopoda)
Identifieur interne : 000385 ( Ncbi/Merge ); précédent : 000384; suivant : 000386An intron-containing, heat-inducible stress-70 gene in the millipede Tachypodoiulus niger (Julidae, Diplopoda)
Auteurs : Thomas Knigge [France] ; Lutz Bachmann [Norvège] ; Heinz-R. Köhler [Allemagne]Source :
- Cell Stress & Chaperones [ 1355-8145 ] ; 2014.
Descripteurs français
- Wicri :
- geographic : Niger.
English descriptors
- KwdEn :
- 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
Url:
DOI: 10.1007/s12192-014-0494-7
PubMed: 24446070
PubMed Central: 4147066
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PMC:4147066Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>The highly conserved part of the nucleotide-binding domain of the <italic>hsp70</italic>
gene family was amplified from the soil diplopod <italic>Tachypodoiulus niger</italic>
(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 (<italic>hsp70</italic>
), the corresponding 70 kDa heat shock cognate (<italic>hsc70</italic>
) and a glucose-related <italic>hsp70</italic>
homologue (<italic>grp78</italic>
). Comparisons of genomic and cDNA sequences of <italic>hsc70</italic>
identified two introns within the consensus sequence. Generally, <italic>stress-70</italic>
expression levels were low, which hampered successful RT-PCR and subsequent subcloning. Following experimental heat shock, however, the spliced <italic>hsc70</italic>
was amplified predominantly, instead of its inducible homologue <italic>hsp70</italic>
. 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. <italic>hsc70</italic>
, albeit having introns, apparently is inducible and contributes to the stress-70 response.</p>
</div>
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<author><name sortKey="Knigge, Thomas" sort="Knigge, Thomas" uniqKey="Knigge T" first="Thomas" last="Knigge">Thomas Knigge</name>
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<front><div type="abstract" xml:lang="en"><p>The highly conserved part of the nucleotide-binding domain of the <italic>hsp70</italic>
gene family was amplified from the soil diplopod <italic>Tachypodoiulus niger</italic>
(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 (<italic>hsp70</italic>
), the corresponding 70 kDa heat shock cognate (<italic>hsc70</italic>
) and a glucose-related <italic>hsp70</italic>
homologue (<italic>grp78</italic>
). Comparisons of genomic and cDNA sequences of <italic>hsc70</italic>
identified two introns within the consensus sequence. Generally, <italic>stress-70</italic>
expression levels were low, which hampered successful RT-PCR and subsequent subcloning. Following experimental heat shock, however, the spliced <italic>hsc70</italic>
was amplified predominantly, instead of its inducible homologue <italic>hsp70</italic>
. 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. <italic>hsc70</italic>
, albeit having introns, apparently is inducible and contributes to the stress-70 response.</p>
</div>
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<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>
</keywords>
<keywords scheme="Wicri" type="geographic" xml:lang="fr"><term>Niger</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
</pubmed>
</double>
</record>
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