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Titolo:
PLANT NUCLEAR-PROTEIN P56 AND ITS ELICITOR-DEPENDENT TRANSIENT BIOSYNTHESIS
Autore:
SCHWER B; KINDL H;
Indirizzi:
UNIV MARBURG,FACHBEREICH CHEM,HANS MEERWEIN STR D-35032 MARBURG GERMANY UNIV MARBURG,FACHBEREICH CHEM,HANS MEERWEIN STR D-35032 MARBURG GERMANY
Titolo Testata:
Protoplasma
fascicolo: 3-4, volume: 176, anno: 1993,
pagine: 165 - 173
SICI:
0033-183X(1993)176:3-4<165:PNPAIE>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PORE COMPLEX; ENDOPLASMIC-RETICULUM; LOCALIZATION; ENVELOPE; BINDING; CELL; IDENTIFICATION; CHITINASE; INDUCTION; CUCUMBER;
Keywords:
ARACHIS-HYPOGAEA; ELICITOR-DEPENDENT SYNTHESIS; NUCLEAR PROTEIN; PROTEIN SYNTHESIS IN-VIVO; SOLUBILIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
B. Schwer e H. Kindl, "PLANT NUCLEAR-PROTEIN P56 AND ITS ELICITOR-DEPENDENT TRANSIENT BIOSYNTHESIS", Protoplasma, 176(3-4), 1993, pp. 165-173

Abstract

Pulse labelling experiments with [S-35]L-methionine were performed todetermine the rate of protein synthesis. Treatment of cultured cells of peanut with fungal cell wall led to a drastic increase in the de novo synthesis of particular proteins in the cytosol, the endoplasmic reticulum and the extracellular compartment. In the nucleus, a single newly synthesized protein, designated p 56, was detectable upon elicitation by fungal elicitor. Pulse labelling with [S-35]L-methionine for 1 h was applied at various times following elicitation. The time course of p 56 biosynthesis was transient and the maximum of p 56 de novo synthesis preceded the one of the cytosolic protein stilbene synthase. The preferential de novo synthesis and transfer of p 56 to the nucleus, only briefly before the elicitor-triggered signal chain causes the activation of nuclear defence genes, makes it a good candidate as member of the signal transduction machinery to the nucleus. p 56 was further characterized by its size as N-octyl-beta-D-glucoside micelle. Selective solubilization experiments showed that p 56 is a hydrophobic, not salt extractable protein rather well protected against partial proteolysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 07:02:46