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Titolo:
The chaperoning activity of hsp110 - Identification of functional domains by use of targeted deletions
Autore:
Oh, HJ; Easton, D; Murawski, M; Kaneko, Y; Subjeck, JR;
Indirizzi:
Roswell Pk Canc Inst, Dept Mol & Cellular Biophys, Buffalo, NY 14263 USA Roswell Pk Canc Inst Buffalo NY USA 14263 Biophys, Buffalo, NY 14263 USA SUNY Coll Buffalo, Dept Biol, Buffalo, NY 14222 USA SUNY Coll Buffalo Buffalo NY USA 14222 , Dept Biol, Buffalo, NY 14222 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 22, volume: 274, anno: 1999,
pagine: 15712 - 15718
SICI:
0021-9258(19990528)274:22<15712:TCAOH->2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT-SHOCK-PROTEIN; SECONDARY STRUCTURE PREDICTION; REGULATED STRESS PROTEIN; PEPTIDE-BINDING DOMAIN; AMINO-ACID-ANALOGS; ENDOPLASMIC-RETICULUM; MOLECULAR CHAPERONES; NONNATIVE PROTEIN; SUBSTRATE-BINDING; LARGE HSP70-LIKE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Subjeck, JR Roswell Pk Canc Inst, Dept Mol & Cellular Biophys, Buffalo, NY14263 USA Roswell Pk Canc Inst Buffalo NY USA 14263 ffalo, NY 14263 USA
Citazione:
H.J. Oh et al., "The chaperoning activity of hsp110 - Identification of functional domains by use of targeted deletions", J BIOL CHEM, 274(22), 1999, pp. 15712-15718

Abstract

hsp110 is one of major heat shock proteins of eukaryotic cells and is a diverged relative of the hsp70 family. It has been previously shown that hsp110 maintains heat-denatured luciferase in a soluble, folding competent state and also confers cellular heat resistance in vivo. In the present study the functional domains of hsp110 that are responsible for its chaperoning activity are identified by targeted deletion mutagenesis using the DnaK structure as the model. The chaperoning activity of mutants is assessed based ontheir ability to solubilize heat-denatured luciferase as well as to refoldluciferase in the presence of rabbit reticulocyte lysate. It is shown thatthese functions require only an internal region of hsp110 that includes the predicted peptide binding domain and two immediately adjacent C-terminal domains. It is also shown that although hsp110 binds ATP, binding can be blocked by its C-terminal region.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 07:49:07