| dc.contributor.author |
Torres, JH |
en |
| dc.contributor.author |
Papandreou, N |
en |
| dc.contributor.author |
Chomilier, J |
en |
| dc.date.accessioned |
2014-06-06T06:49:31Z |
|
| dc.date.available |
2014-06-06T06:49:31Z |
|
| dc.date.issued |
2009 |
en |
| dc.identifier.issn |
13558145 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1007/s12192-008-0083-8 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4648 |
|
| dc.subject |
Hop |
en |
| dc.subject |
Hsp organizing protein |
en |
| dc.subject |
Hsp70 interacting protein |
en |
| dc.subject |
Hydrophobic cluster analysis |
en |
| dc.subject |
Tetratricopeptide repeat |
en |
| dc.subject |
Tpr protein |
en |
| dc.subject.other |
bacterial protein |
en |
| dc.subject.other |
chaperone |
en |
| dc.subject.other |
dipeptide |
en |
| dc.subject.other |
heat shock protein 70 interacting protein |
en |
| dc.subject.other |
heat shock protein organizing protein |
en |
| dc.subject.other |
microorganism protein |
en |
| dc.subject.other |
protein GerD |
en |
| dc.subject.other |
tetratricopeptide repeat protein |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
heat shock protein 70 |
en |
| dc.subject.other |
heat shock protein 90 |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
cluster analysis |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
DNA flanking region |
en |
| dc.subject.other |
eukaryote |
en |
| dc.subject.other |
gene structure |
en |
| dc.subject.other |
genetic recombination |
en |
| dc.subject.other |
hydrophobicity |
en |
| dc.subject.other |
intron |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
nucleotide sequence |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
prokaryote |
en |
| dc.subject.other |
protein domain |
en |
| dc.subject.other |
protein family |
en |
| dc.subject.other |
sequence analysis |
en |
| dc.subject.other |
amino acid sequence |
en |
| dc.subject.other |
animal |
en |
| dc.subject.other |
eukaryotic cell |
en |
| dc.subject.other |
genetics |
en |
| dc.subject.other |
human |
en |
| dc.subject.other |
metabolism |
en |
| dc.subject.other |
molecular evolution |
en |
| dc.subject.other |
molecular genetics |
en |
| dc.subject.other |
physiology |
en |
| dc.subject.other |
prokaryotic cell |
en |
| dc.subject.other |
protein secondary structure |
en |
| dc.subject.other |
protein tertiary structure |
en |
| dc.subject.other |
Eukaryota |
en |
| dc.subject.other |
Prokaryota |
en |
| dc.subject.other |
Amino Acid Sequence |
en |
| dc.subject.other |
Animals |
en |
| dc.subject.other |
Eukaryotic Cells |
en |
| dc.subject.other |
Evolution, Molecular |
en |
| dc.subject.other |
HSP70 Heat-Shock Proteins |
en |
| dc.subject.other |
HSP90 Heat-Shock Proteins |
en |
| dc.subject.other |
Humans |
en |
| dc.subject.other |
Introns |
en |
| dc.subject.other |
Molecular Chaperones |
en |
| dc.subject.other |
Molecular Sequence Data |
en |
| dc.subject.other |
Prokaryotic Cells |
en |
| dc.subject.other |
Protein Structure, Secondary |
en |
| dc.subject.other |
Protein Structure, Tertiary |
en |
| dc.subject.other |
Sequence Analysis, Protein |
en |
| dc.title |
Sequence analyses reveal that a TPR-DP module, surrounded by recombinable flanking introns, could be at the origin of eukaryotic Hop and Hip TPR-DP domains and prokaryotic GerD proteins |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1007/s12192-008-0083-8 |
en |
| heal.publicationDate |
2009 |
en |
| heal.abstract |
The co-chaperone Hop [heat shock protein (HSP) organising protein] is known to bind both Hsp70 and Hsp90. Hop comprises three repeats of a tetratricopeptide repeat (TPR) domain, each consisting of three TPR motifs. The first and last TPR domains are followed by a domain containing several dipeptide (DP) repeats called the DP domain. These analyses suggest that, the hop genes result from successive recombination events of an ancestral TPRDP module. From a hydrophobic cluster analysis of homologous Hop protein sequences derived from gene families, we can postulate that shins in the open reading frames are at the origin of the present sequences. Moreover, these shifts can be related to the presence or absence of biological function. We propose to extend the family of Hop co-chaperons into the kingdom of bacteria, as several structurally related genes have been identified by hydrophobic cluster analysis. We also provide evidence of common, structural characteristics between hop and hip genes, suggesting a shared precursor of ancestral TPR-DP domains. |
en |
| heal.journalName |
Cell Stress and Chaperones |
en |
| dc.identifier.issue |
3 |
en |
| dc.identifier.volume |
14 |
en |
| dc.identifier.doi |
10.1007/s12192-008-0083-8 |
en |
| dc.identifier.spage |
281 |
en |
| dc.identifier.epage |
289 |
en |