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Titolo:
ATP and the core "alpha-crystallin" domain of the small heat-shock proteinalpha B-crystallin
Autore:
Muchowski, PJ; Hays, LG; Yates, JR; Clark, JI;
Indirizzi:
Univ Washington, Dept Biol Struct, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 t Biol Struct, Seattle, WA 98195 USA Univ Washington, Dept Mol Biotechnol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ol Biotechnol, Seattle, WA 98195 USA Univ Washington, Dept Ophthalmol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 pt Ophthalmol, Seattle, WA 98195 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 42, volume: 274, anno: 1999,
pagine: 30190 - 30195
SICI:
0021-9258(19991015)274:42<30190:AATC"D>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHAPERONE-LIKE ACTIVITY; INDUCED CONFORMATIONAL-CHANGES; LIMITED PROTEOLYTIC SITES; MOLECULAR CHAPERONE; A-CRYSTALLIN; ALZHEIMERS-DISEASE; MASS-SPECTROMETRY; MISSENSE MUTATION; LENS CRYSTALLINS; BINDING DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
73
Recensione:
Indirizzi per estratti:
Indirizzo: Clark, JI Univ Washington, Dept Biol Struct, Box 357420, Seattle, WA 98195USA Univ Washington Box 357420 Seattle WA USA 98195 le, WA 98195 USA
Citazione:
P.J. Muchowski et al., "ATP and the core "alpha-crystallin" domain of the small heat-shock proteinalpha B-crystallin", J BIOL CHEM, 274(42), 1999, pp. 30190-30195

Abstract

Electrospray ionization mass spectrometry (ESI-LC/MS) of tryptic digests of human alpha B-crystallin in the presence and absence of ATP identified four residues located within the core "alpha-crystallin" domain, Lys(82), Lys(103), Arg(116), and Arg(123) that were shielded from the action of trypsinin the presence of ATP. In control experiments, chymotrypsin was used in place of trypsin. The chymotryptic fragments of human alpha B-crystallin produced in the presence and absence of ATP were analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS), Seven chymotryptic cleavage sites, Trp(60), Phe(61), Phe(75), Phe(84), Phe(113), Phe(118), and Tyr(122), located near or within the core alpha-crystallin domain, were shielded fromthe action of chymotrypsin in the presence of ATP. Chemically similar analogs of ATP were less protective than ATP against proteolysis by trypsin or chymotrypsin. ATP had no effect on the enzymatic: activity of trypsin and the K-m for trypsin was 0.031 mM in the presence of ATP and 0.029 mM in the absence of ATP. The results demonstrated an ATP-de; pendent structural modification in the Gore alpha-crystallin domain conserved in nearly all identified small heat-shock proteins that act as molecular chaperones.

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Documento generato il 16/07/20 alle ore 16:41:56