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Titolo:
The chloroplast 22-Ku heat-shock protein: A lumenal protein that associates with the oxygen evolving complex and protects photosystem II during heat stress
Autore:
Downs, CA; Coleman, JS; Heckathorn, SA;
Indirizzi:
Coll Charleston, Dept Biol, Charleston, SC 29424 USA Coll Charleston Charleston SC USA 29424 pt Biol, Charleston, SC 29424 USA Syracuse Univ, Dept Biol, Syracuse, NY 13244 USA Syracuse Univ Syracuse NY USA 13244 iv, Dept Biol, Syracuse, NY 13244 USA
Titolo Testata:
JOURNAL OF PLANT PHYSIOLOGY
fascicolo: 4-5, volume: 155, anno: 1999,
pagine: 477 - 487
SICI:
0176-1617(199910)155:4-5<477:TC2HPA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-TRANSPORT CHAIN; CHAPERONE-LIKE ACTIVITY; ALPHA-B-CRYSTALLIN; THYLAKOID MEMBRANES; HIGH-TEMPERATURE; NONTOLERANT VARIANTS; CO2 ASSIMILATION; HIGHER-PLANTS; YOUNG LEAVES; THERMOTOLERANCE;
Keywords:
Chenopodium album (L.); small heat-shock protein; chloroplast; Photosystem II; heat stress; photosynthesis; thermotolerance;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
73
Recensione:
Indirizzi per estratti:
Indirizzo: Downs, CA Coll Charleston, Dept Biol, 58 Coming St, Charleston, SC 29424 USA Coll Charleston 58 Coming St Charleston SC USA 29424 C 29424 USA
Citazione:
C.A. Downs et al., "The chloroplast 22-Ku heat-shock protein: A lumenal protein that associates with the oxygen evolving complex and protects photosystem II during heat stress", J PLANT PHY, 155(4-5), 1999, pp. 477-487

Abstract

An evolutionarily conserved small heat-shock protein localizes to the chloroplast (chlpsHsp) in all major phyla of terrestrial plants examined to date. The chlpsHsp is known to protect photosynthetic electron transport, specifically that of Photosystem II, during heat stress. Suborganellar examination indicated that there are two forms of the chlpsHsp, a 25-Ku and a 22-Kuform. Protease treatment of isolated subchloroplast fractions (thylakoid grana vs, stroma) demonstrated that the 22-Ku chlpsHsp form is found in the thylakoid lumen. Co-immunoprecipitation of the chlpsHsp using a concentration of Triton X-100 below its critical micelle concentration showed that this protein associates with proteins of Photosystem II. Coimmunoprecipitationof the chlpsHsp using a concentration of Triton X-100 significantly above its critical micelle concentration showed that this protein specifically interacts with proteins of the thermolabile Oxygen Evolving Complex of Photosystem II. The chlpsHsp does not reactivate heat-denatured Photosystem II, bur instead protects this complex from damage during heat stress.

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Documento generato il 25/01/20 alle ore 16:30:59