Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function.
J Exp Zool B Mol Dev Evol
; 322(6): 359-78, 2014 Sep.
Article
en En
| MEDLINE
| ID: mdl-24106212
Molecular chaperones and their associated co-chaperones play an important role in preserving and regulating the active conformational state of cellular proteins. The chaperone complement of the Indonesian Coelacanth, Latimeria menadoensis, was elucidated using transcriptomic sequences. Heat shock protein 90 (Hsp90) and heat shock protein 40 (Hsp40) chaperones, and associated co-chaperones were focused on, and homologous human sequences were used to search the sequence databases. Coelacanth homologs of the cytosolic, mitochondrial and endoplasmic reticulum (ER) homologs of human Hsp90 were identified, as well as all of the major co-chaperones of the cytosolic isoform. Most of the human Hsp40s were found to have coelacanth homologs, and the data suggested that all of the chaperone machinery for protein folding at the ribosome, protein translocation to cellular compartments such as the ER and protein degradation were conserved. Some interesting similarities and differences were identified when interrogating human, mouse, and zebrafish homologs. For example, DnaJB13 is predicted to be a non-functional Hsp40 in humans, mouse, and zebrafish due to a corrupted histidine-proline-aspartic acid (HPD) motif, while the coelacanth homolog has an intact HPD. These and other comparisons enabled important functional and evolutionary questions to be posed for future experimental studies.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
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Chaperonas Moleculares
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Proteínas HSP90 de Choque Térmico
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Proteínas del Choque Térmico HSP40
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Peces
Límite:
Animals
Idioma:
En
Revista:
J Exp Zool B Mol Dev Evol
Año:
2014
Tipo del documento:
Article
País de afiliación:
Turquía
Pais de publicación:
Estados Unidos