Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function

Tastan Bishop, Özlem; Edkins, Adrienne L; Blatch, Gregory L

Title: Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function
Creator: Tastan Bishop, Özlem
Creator: Edkins, Adrienne L
Creator: Blatch, Gregory L
Date Issued: 2014
Date: 2014
Type: text
Type: article
Identifier: http://hdl.handle.net/10962/126932
Identifier: vital:35936
Identifier: https://doi.10.1002/jez.b.22541
Description: 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 cochaperones 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.
Format: 20 pages
Format: pdf
Language: English
Relation: Journal of experimental zoology part B: molecular and developmental evolution
Relation: Tastan Bishop, Ö., Edkins, A.L. and Blatch, G.L., 2014. Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function. Journal of Experimental Zoology Part B: Molecular and Developmental Evolution, 322(6), pp.359-378
Relation: Journal of experimental zoology part B: molecular and developmental evolution volume 322 number 6 359 378 2014 1552-5007
Rights: Journal of Experimental zoology part B: molecular and developmental evolution
Rights: Use of this resource is governed by the terms and conditions of the Wiley Online Library Terms of Use statement (https://onlinelibrary.wiley.com/terms-and-conditions)

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Tastan Bishop, Ozlem (Prof)

RU Research Unit in Bioinformatics (RUBi)

RU Department of Biochemistry, Microbiology and Biotechnology

Blatch, Gregory Lloyd (Prof)

Edkins, Adrienne Lesley (Associate Prof)

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