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Titolo:
TRANSPORT AND DEPOSITION OF CEREAL PROLAMINS
Autore:
RICHARD G; TURNER MPF; NAPIER JA; SHEWRY PR;
Indirizzi:
UNIV BRISTOL,LONG ASHTON RES STN,DEPT AGR SCI,IARC BRISTOL BS18 9AF AVON ENGLAND UNIV BRISTOL,LONG ASHTON RES STN,DEPT AGR SCI,IARC BRISTOL BS18 9AF AVON ENGLAND
Titolo Testata:
Plant physiology and biochemistry
fascicolo: 2, volume: 34, anno: 1996,
pagine: 237 - 243
SICI:
0981-9428(1996)34:2<237:TADOCP>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEVELOPING BARLEY ENDOSPERM; TRANSGENIC TOBACCO SEEDS; WHEAT TRITICUM-AESTIVUM; LYSINE-CONTAINING ZEINS; PROTEIN-BODY FORMATION; ENDOPLASMIC-RETICULUM; STORAGE PROTEINS; IMMUNOCYTOCHEMICAL LOCALIZATION; XENOPUS OOCYTES; MAIZE ENDOSPERM;
Keywords:
CEREALS; STORAGE PROTEINS; PROLAMINS; WHEAT; TRAFFICKING; PROTEIN BODIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
G. Richard et al., "TRANSPORT AND DEPOSITION OF CEREAL PROLAMINS", Plant physiology and biochemistry, 34(2), 1996, pp. 237-243

Abstract

The alcohol-soluble storage proteins of cereal grains, called prolamins, are synthesised on rough endoplasmic reticulum (ER) in the developing starchy endosperm cells and deposited in discrete protein bodies. Two pathways of protein body formation have been proposed: transport via the Golgi apparatus to the vacuole, or direct accumulation within the ER. We discuss and evaluate the evidence for these two pathways, including results of immunoelectron microscopy, characterization of isolated organelles and expression of wild type and mutant proteins in heterologous systems (yeast, Xenopus oocytes and transgenic tobacco). Theconclusion is that both pathways may operate, either in different species or in the same tissue at the same or different stages of development. We also discuss the mechanisms which may determine the sorting and trafficking of prolamins within the secretory system, including the roles of ER retention and vacuolar targeting sequences and of molecular chaperones of the HSP70/BiP family, and the organisation of prolamins within the protein body.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:02:12