Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Molecular cloning of horse Hsp90 cDNA and its comparative analysis with other vertebrate Hsp90 sequences
Autore:
Pepin, K; Momose, F; Ishida, N; Nagata, K;
Indirizzi:
JRA, Equine Res Inst, Mol & Cellular Biol Lab, Utsunomiya, Tochigi 3200856, Japan JRA Utsunomiya Tochigi Japan 3200856 , Utsunomiya, Tochigi 3200856, Japan
Titolo Testata:
JOURNAL OF VETERINARY MEDICAL SCIENCE
fascicolo: 2, volume: 63, anno: 2001,
pagine: 115 - 124
SICI:
0916-7250(200102)63:2<115:MCOHHC>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT-SHOCK-PROTEIN; GLUCOCORTICOID RECEPTOR; CHAPERONE ACTIVITY; SIGNAL TRANSDUCER; TERMINAL DOMAIN; IN-VIVO; BINDING; COMPLEX; HEAT-SHOCK-PROTEIN-90; CONFORMATION;
Keywords:
heat shock protein; Hsp90; phylogenetic analysis; sequence comparison;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Nagata, K Tokyo Inst Technol, Grad Sch Biosci & Biotechnool, Dept Biol Informat, LabMol Med Engn, Yokohama, Kanagawa 2268501, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 2268501 68501, Japan
Citazione:
K. Pepin et al., "Molecular cloning of horse Hsp90 cDNA and its comparative analysis with other vertebrate Hsp90 sequences", J VET MED S, 63(2), 2001, pp. 115-124

Abstract

Heat shock protein 90 (Hsp90), a molecular chaperone, is ubiquitous and involved in numerous cellular processes. To contribute to the relatively small collection of vertebrate Hsp90 sequences in the gene data bank, we clonedand sequenced horse (Equus caballus) Hsp90 alpha and beta cDNAs. This enabled identification of horse-specific primers for development of a convenient PCR-based method that could monitor horse stress tolerance. We analyzed the sequence data comparatively and phylogenetically with other Hsp90 cDNA sequences, and identified vertebrate-specific and isoform-specific conservedregions to facilitate future molecular investigations of Hsp90 functions. We found 4 highly conserved regions to vertebrate Hsp90 exclusively and 27 amino acids conserved among but differing between Hsp90 alpha and Hsp90 beta sequences. Protein-based phylogenetic trees revealed high conservation between mammal species within Hsp90 alpha and beta clusters. Comparison of nucleotide and amino acid substitution levels suggests that horse Hsp90 beta has undergone strong purifying selection, while rat Hsp90 beta and hamster Hsp90 alpha have been positively selected. Surprisingly, fish Hsp90 alpha genes clearly clustered with Hsp90 beta genes, and no distinct placement of fish Hsp90 alpha protein was found. The Hsp90 alpha isoform is apparently the result of beta gene duplication. Our results highlight the importance oforganism- and isoform-specific Hsp90 functional analyses in describing therole of Hsp90 in describing the role of Hsp90 in cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 22:15:41